T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction

Shi, Ke; Bohl, Thomas E.; Park, Jeonghyun; Zasada, Andrew; Malik, Shray; Banerjee, Surajit; Tran, Vincent; Li, Na; Yin, Zhiqi; Kurniawan, Fredy; Orellana, Kayo; Aihara, Hideki

doi:10.1093/nar/gky776

Title: T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction

Full Record
Other Related Research

Authors:

Shi, Ke ^[1]; Bohl, Thomas E. ^[1]; Park, Jeonghyun ^[1]; Zasada, Andrew ^[1]; Malik, Shray ^[1]; Banerjee, Surajit ^[2]; Tran, Vincent ^[1]; Li, Na ^[1]; Yin, Zhiqi ^[1]; Kurniawan, Fredy ^[1]; Orellana, Kayo ^[1];

^[1]

Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, 6–155 Jackson Hall, 321 Church Street S.E. Minneapolis, MN 55455, USA
Northeastern Collaborative Access Team, Cornell University, Advanced Photon Source, Lemont, Illinois, 60439, USA

Publication Date:: Wed Aug 29 00:00:00 EDT 2018

Sponsoring Org.:: USDOE

OSTI Identifier:: 1480550

Grant/Contract Number:: AC02-06CH11357

Resource Type:: Published Article

Journal Name:: Nucleic Acids Research

Additional Journal Information:: Journal Name: Nucleic Acids Research Journal Volume: 46 Journal Issue: 19; Journal ID: ISSN 0305-1048

Publisher:: Oxford University Press

Country of Publication:: United Kingdom

Language:: English

Citation Formats


                    Shi, Ke, Bohl, Thomas E., Park, Jeonghyun, Zasada, Andrew, Malik, Shray, Banerjee, Surajit, Tran, Vincent, Li, Na, Yin, Zhiqi, Kurniawan, Fredy, Orellana, Kayo, and Aihara, Hideki. T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction.  United Kingdom: N. p., 2018. 
Web.  doi:10.1093/nar/gky776.

Copy to clipboard


                    Shi, Ke, Bohl, Thomas E., Park, Jeonghyun, Zasada, Andrew, Malik, Shray, Banerjee, Surajit, Tran, Vincent, Li, Na, Yin, Zhiqi, Kurniawan, Fredy, Orellana, Kayo, & Aihara, Hideki. T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction.  United Kingdom.  https://doi.org/10.1093/nar/gky776

Copy to clipboard


                    Shi, Ke, Bohl, Thomas E., Park, Jeonghyun, Zasada, Andrew, Malik, Shray, Banerjee, Surajit, Tran, Vincent, Li, Na, Yin, Zhiqi, Kurniawan, Fredy, Orellana, Kayo, and Aihara, Hideki. Wed .  
"T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction".  United Kingdom.  https://doi.org/10.1093/nar/gky776.

Copy to clipboard


                    
@article{osti_1480550,

  title        = {T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction},

  author       = {Shi, Ke and Bohl, Thomas E. and Park, Jeonghyun and Zasada, Andrew and Malik, Shray and Banerjee, Surajit and Tran, Vincent and Li, Na and Yin, Zhiqi and Kurniawan, Fredy and Orellana, Kayo and Aihara, Hideki},

  abstractNote = {},

  doi          = {10.1093/nar/gky776},

  journal      = {Nucleic Acids Research},

  number       = 19,

  volume       = 46,

  place        = {United Kingdom},

  year         = {Wed Aug 29 00:00:00 EDT 2018},

  month        = {Wed Aug 29 00:00:00 EDT 2018}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Publisher's Version of Record
https://doi.org/10.1093/nar/gky776

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 29 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction

Journal Article Shi, Ke ; Bohl, Thomas E. ; Park, Jeonghyun ; ... - Nucleic Acids Research
https://doi.org/10.1093/nar/gky776
Structures of ATP-bound DNA ligase D in a closed domain conformation reveal a network of amino acid and metal contacts to the ATP phosphates

Journal Article Unciuleac, Mihaela-Carmen ; Goldgur, Yehuda ; Shuman, Stewart - Journal of Biological Chemistry

DNA ligases are the sine qua non of genome integrity and essential for DNA replication and repair in all organisms. DNA ligases join 3'-OH and 5'-PO₄ ends via a series of three nucleotidyl transfer steps. In step 1, ligase reacts with ATP or NAD⁺ to form a covalent ligase-(lysyl-Nmore »« less
Cited by 8
https://doi.org/10.1074/jbc.RA119.007445

Full Text Available
Bleomycin-induced DNA repair by Saccharomyces cerevisiae ATP-dependent polydeoxyribonucleotide ligase

Journal Article Moore, C W - Journal of Bacteriology; (USA)

In contrast to ligase-deficient (cdc9) Saccharomyces cerevisiae, which did not rejoin bleomycin-induced DNA breaks, ligase-proficient (CDC9) yeast cells eliminated approximately 90% of DNA breaks within 90 to 120 min after treatment. Experimental conditions restricted enzymatic removal of the unusual 3{prime}-phosphoglycolate terminal in DNA cleaved by bleomycin and involved doses producing equivalent numbers of DNA breaks or doses producing equivalent killing.
Structural Studies of a Bacterial Condensin Complex Reveal ATP-Dependent Disruption of Intersubunit Interactions

Journal Article Woo, J ; Lim, J ; Shin, H ; ... - Cell

Condensins are key mediators of chromosome condensation across organisms. Like other condensins, the bacterial MukBEF condensin complex consists of an SMC family protein dimer containing two ATPase head domains, MukB, and two interacting subunits, MukE and MukF. We report complete structural views of the intersubunit interactions of this condensin along with ensuing studies that reveal a role for the ATPase activity of MukB. MukE and MukF together form an elongated dimeric frame, and MukF's C-terminal winged-helix domains (C-WHDs) bind MukB heads to constitute closed ring-like structures. Surprisingly, one of the two bound C-WHDs is forced to detach upon ATP-mediated engagementmore »« less
https://doi.org/10.1016/j.cell.2008.10.050
Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions

Journal Article Woo, J S ; Robinson, H ; Lim, J H ; ... - Cell
https://doi.org/10.1016/j.cell.2008.10.050

Similar Records