Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase

Li, Baobin; Li, Hao; Hu, Chia-Wei; Jiang, Jiaoyang

doi:10.1038/s41467-017-00865-1

Title: Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase

Abstract

The O-linked β-N-acetyl glucosamine (O-GlcNAc) modification dynamically regulates the functions of numerous proteins. A single human enzyme O-linked β-N-acetyl glucosaminase (O-GlcNAcase or OGA) hydrolyzes this modification. To date, it remains largely unknown how OGA recognizes various substrates. Here we report the structures of OGA in complex with each of four distinct glycopeptide substrates that contain a single O-GlcNAc modification on a serine or threonine residue. Intriguingly, these glycopeptides bind in a bidirectional yet conserved conformation within the substrate-binding cleft of OGA. This study provides fundamental insights into a general principle that confers the substrate binding adaptability and specificity to OGA in O-GlcNAc regulation.

Authors:

Li, Baobin ^[1];

^[1]; Hu, Chia-Wei ^[1]; Jiang, Jiaoyang ^[1]

Univ. of Wisconsin, Madison, WI (United States)

Publication Date:: Fri Sep 22 00:00:00 EDT 2017

Research Org.:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Org.:: USDOE

OSTI Identifier:: 1438911

Resource Type:: Accepted Manuscript

Journal Name:: Nature Communications

Additional Journal Information:: Journal Volume: 8; Journal Issue: 1; Journal ID: ISSN 2041-1723

Publisher:: Nature Publishing Group

Country of Publication:: United States

Language:: ENGLISH

Subject:: 59 BASIC BIOLOGICAL SCIENCES; Glycobiology; X-ray crystallography

Citation Formats


                    Li, Baobin, Li, Hao, Hu, Chia-Wei, and Jiang, Jiaoyang. Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase.  United States: N. p., 2017. 
Web.  doi:10.1038/s41467-017-00865-1.

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                    Li, Baobin, Li, Hao, Hu, Chia-Wei, & Jiang, Jiaoyang. Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase.  United States.  https://doi.org/10.1038/s41467-017-00865-1

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                    Li, Baobin, Li, Hao, Hu, Chia-Wei, and Jiang, Jiaoyang. Fri .  
"Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase".  United States.  https://doi.org/10.1038/s41467-017-00865-1.  https://www.osti.gov/servlets/purl/1438911.

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@article{osti_1438911,

  title        = {Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase},

  author       = {Li, Baobin and Li, Hao and Hu, Chia-Wei and Jiang, Jiaoyang},

  abstractNote = {The O-linked β-N-acetyl glucosamine (O-GlcNAc) modification dynamically regulates the functions of numerous proteins. A single human enzyme O-linked β-N-acetyl glucosaminase (O-GlcNAcase or OGA) hydrolyzes this modification. To date, it remains largely unknown how OGA recognizes various substrates. Here we report the structures of OGA in complex with each of four distinct glycopeptide substrates that contain a single O-GlcNAc modification on a serine or threonine residue. Intriguingly, these glycopeptides bind in a bidirectional yet conserved conformation within the substrate-binding cleft of OGA. This study provides fundamental insights into a general principle that confers the substrate binding adaptability and specificity to OGA in O-GlcNAc regulation.},

  doi          = {10.1038/s41467-017-00865-1},

  journal      = {Nature Communications},

  number       = 1,

  volume       = 8,

  place        = {United States},

  year         = {Fri Sep 22 00:00:00 EDT 2017},

  month        = {Fri Sep 22 00:00:00 EDT 2017}

}

Copy to clipboard

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https://doi.org/10.1038/s41467-017-00865-1

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate
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Lazarus, Michael B.; Nam, Yunsun; Jiang, Jiaoyang
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Nature Chemical Biology, Vol. 13, Issue 6
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Yuzwa, Scott A.; Macauley, Matthew S.; Heinonen, Julia E.
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Works referencing / citing this record:

Chemical and Biochemical Strategies To Explore the Substrate Recognition of O ‐GlcNAc‐Cycling Enzymes
journal, November 2018

Hu, Chia‐Wei; Worth, Matthew; Li, Hao
ChemBioChem, Vol. 20, Issue 3
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Structural studies of a surface-entropy reduction mutant of O-GlcNAcase
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Ezeudu, Florence Obiageli; Eya, Ngozi M.; Nwafor, Stephen Chinedu
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Hart, Gerald W.
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Title: Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase

Abstract

Citation Formats

Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode journal, March 2017

Refinement of Macromolecular Structures by the Maximum-Likelihood Method journal, May 1997

Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity journal, March 2006

Coot model-building tools for molecular graphics journal, November 2004

Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis journal, March 2006

Structural snapshots of the reaction coordinate for O-GlcNAc transferase journal, October 2012

Dynamic O -Glycosylation of Nuclear and Cytosolic Proteins : CLONING AND CHARACTERIZATION OF A NEUTRAL, CYTOSOLIC β- journal, January 2001

A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo journal, June 2008

Analysis of PUGNAc and NAG-thiazoline as Transition State Analogues for Human O -GlcNAcase: Mechanistic and Structural Insights into Inhibitor Selectivity and Transition State Poise journal, January 2007

The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α journal, September 2004

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Dynamic Glycosylation of Nuclear and Cytosolic Proteins: CLONING AND CHARACTERIZATION OF A UNIQUE journal, April 1997

Structure of human O-GlcNAc transferase and its complex with a peptide substrate journal, January 2011

The active site of O-GlcNAc transferase imposes constraints on substrate sequence journal, August 2015

Protein O-GlcNAcylation: emerging mechanisms and functions journal, May 2017

PHENIX : building new software for automated crystallographic structure determination journal, October 2002

Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins journal, April 2007

O -GlcNAcase Uses Substrate-assisted Catalysis : KINETIC ANALYSIS AND DEVELOPMENT OF HIGHLY SELECTIVE MECHANISM-INSPIRED INHIBITORS journal, March 2005

Structural and functional insight into human O-GlcNAcase journal, March 2017

Insights into activity and inhibition from the crystal structure of human O-GlcNAcase journal, March 2017

O -GlcNAcase: Promiscuous Hexosaminidase or Key Regulator of O -GlcNAc Signaling? journal, October 2014

O -Linked GlcNAc Transferase Is a Conserved Nucleocytoplasmic Protein Containing Tetratricopeptide Repeats journal, April 1997

A Novel Quantitative Mass Spectrometry Platform for Determining Protein O-GlcNAcylation Dynamics journal, April 2016

[20] Processing of X-ray diffraction data collected in oscillation mode book, January 1997

Evidence for a Functional O -Linked N -Acetylglucosamine ( O -GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum journal, October 2015

Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition journal, February 2012

Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition journal, February 2012

Visualizing the Reaction Coordinate of an O-GlcNAc Hydrolase journal, February 2010

Structure of human O-GlcNAc transferase and its complex with a peptide substrate journal, January 2011

Insights into activity and inhibition from the crystal structure of human O-GlcNAcase journal, March 2017

Structural and functional insight into human O-GlcNAcase journal, March 2017

A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo journal, June 2008

Protein O-GlcNAcylation: emerging mechanisms and functions journal, May 2017

The active site of O-GlcNAc transferase imposes constraints on substrate sequence journal, August 2015

Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity journal, March 2006

The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α journal, September 2004

Human OGA binds substrates in a conserved peptide recognition groove journal, October 2010

Chemical and Biochemical Strategies To Explore the Substrate Recognition of O ‐GlcNAc‐Cycling Enzymes journal, November 2018

Nutrient regulation of signaling and transcription journal, January 2019

Structural studies of a surface-entropy reduction mutant of O-GlcNAcase journal, January 2019

Crosstalk between phosphorylation and O‐Glc NA cylation: friend or foe journal, May 2018

Intervention for depression among chemistry education undergraduates in a Nigerian university journal, July 2019

Nutrient Regulation of Signaling and Transcription journal, April 2018

Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode
journal, March 2017

Refinement of Macromolecular Structures by the Maximum-Likelihood Method
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Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity
journal, March 2006

Coot model-building tools for molecular graphics
journal, November 2004

Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis
journal, March 2006

Structural snapshots of the reaction coordinate for O-GlcNAc transferase
journal, October 2012

Dynamic O -Glycosylation of Nuclear and Cytosolic Proteins : CLONING AND CHARACTERIZATION OF A NEUTRAL, CYTOSOLIC β-
journal, January 2001

A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo
journal, June 2008

Analysis of PUGNAc and NAG-thiazoline as Transition State Analogues for Human O -GlcNAcase: Mechanistic and Structural Insights into Inhibitor Selectivity and Transition State Poise
journal, January 2007

The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α
journal, September 2004

Visualizing the Reaction Coordinate of an O-GlcNAc Hydrolase
journal, February 2010

Dynamic Glycosylation of Nuclear and Cytosolic Proteins: CLONING AND CHARACTERIZATION OF A UNIQUE
journal, April 1997

Structure of human O-GlcNAc transferase and its complex with a peptide substrate
journal, January 2011

The active site of O-GlcNAc transferase imposes constraints on substrate sequence
journal, August 2015

Protein O-GlcNAcylation: emerging mechanisms and functions
journal, May 2017

PHENIX : building new software for automated crystallographic structure determination
journal, October 2002

Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
journal, April 2007

O -GlcNAcase Uses Substrate-assisted Catalysis : KINETIC ANALYSIS AND DEVELOPMENT OF HIGHLY SELECTIVE MECHANISM-INSPIRED INHIBITORS
journal, March 2005

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journal, March 2017

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journal, March 2017

O -GlcNAcase: Promiscuous Hexosaminidase or Key Regulator of O -GlcNAc Signaling?
journal, October 2014

O -Linked GlcNAc Transferase Is a Conserved Nucleocytoplasmic Protein Containing Tetratricopeptide Repeats
journal, April 1997

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journal, April 2016

[20] Processing of X-ray diffraction data collected in oscillation mode
book, January 1997

Evidence for a Functional O -Linked N -Acetylglucosamine ( O -GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum
journal, October 2015

Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition
journal, February 2012

Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition
journal, February 2012

Visualizing the Reaction Coordinate of an O-GlcNAc Hydrolase
journal, February 2010

Structure of human O-GlcNAc transferase and its complex with a peptide substrate
journal, January 2011

Insights into activity and inhibition from the crystal structure of human O-GlcNAcase
journal, March 2017

Structural and functional insight into human O-GlcNAcase
journal, March 2017

A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo
journal, June 2008

Protein O-GlcNAcylation: emerging mechanisms and functions
journal, May 2017

The active site of O-GlcNAc transferase imposes constraints on substrate sequence
journal, August 2015

Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity
journal, March 2006

The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α
journal, September 2004

Human OGA binds substrates in a conserved peptide recognition groove
journal, October 2010

Chemical and Biochemical Strategies To Explore the Substrate Recognition of O ‐GlcNAc‐Cycling Enzymes
journal, November 2018

Nutrient regulation of signaling and transcription
journal, January 2019

Structural studies of a surface-entropy reduction mutant of O-GlcNAcase
journal, January 2019

Crosstalk between phosphorylation and O‐Glc NA cylation: friend or foe
journal, May 2018

Intervention for depression among chemistry education undergraduates in a Nigerian university
journal, July 2019

Nutrient Regulation of Signaling and Transcription
journal, April 2018