Structural and Dynamic Basis for Low-Affinity, High-Selectivity Binding of L-Glutamine by the Glutamine Riboswitch

Ren, Aiming; Xue, Yi; Peselis, Alla; Serganov, Alexander; Al-Hashimi, Hashim M.; Patel, Dinshaw J.

doi:10.1016/j.celrep.2015.10.062

Title: Structural and Dynamic Basis for Low-Affinity, High-Selectivity Binding of L-Glutamine by the Glutamine Riboswitch

Full Record
Other Related Research

Authors:: Ren, Aiming; Xue, Yi; Peselis, Alla; Serganov, Alexander; Al-Hashimi, Hashim M.; Patel, Dinshaw J.

Publication Date:: Tue Dec 01 00:00:00 EST 2015

Sponsoring Org.:: USDOE

OSTI Identifier:: 1242319

Resource Type:: Published Article

Journal Name:: Cell Reports

Additional Journal Information:: Journal Name: Cell Reports Journal Volume: 13 Journal Issue: 9; Journal ID: ISSN 2211-1247

Publisher:: Elsevier

Country of Publication:: Netherlands

Language:: English

Citation Formats


                    Ren, Aiming, Xue, Yi, Peselis, Alla, Serganov, Alexander, Al-Hashimi, Hashim M., and Patel, Dinshaw J. Structural and Dynamic Basis for Low-Affinity, High-Selectivity Binding of L-Glutamine by the Glutamine Riboswitch.  Netherlands: N. p., 2015. 
Web.  doi:10.1016/j.celrep.2015.10.062.

Copy to clipboard


                    Ren, Aiming, Xue, Yi, Peselis, Alla, Serganov, Alexander, Al-Hashimi, Hashim M., & Patel, Dinshaw J. Structural and Dynamic Basis for Low-Affinity, High-Selectivity Binding of L-Glutamine by the Glutamine Riboswitch.  Netherlands.  https://doi.org/10.1016/j.celrep.2015.10.062

Copy to clipboard


                    Ren, Aiming, Xue, Yi, Peselis, Alla, Serganov, Alexander, Al-Hashimi, Hashim M., and Patel, Dinshaw J. Tue .  
"Structural and Dynamic Basis for Low-Affinity, High-Selectivity Binding of L-Glutamine by the Glutamine Riboswitch".  Netherlands.  https://doi.org/10.1016/j.celrep.2015.10.062.

Copy to clipboard


                    
@article{osti_1242319,

  title        = {Structural and Dynamic Basis for Low-Affinity, High-Selectivity Binding of L-Glutamine by the Glutamine Riboswitch},

  author       = {Ren, Aiming and Xue, Yi and Peselis, Alla and Serganov, Alexander and Al-Hashimi, Hashim M. and Patel, Dinshaw J.},

  abstractNote = {},

  doi          = {10.1016/j.celrep.2015.10.062},

  journal      = {Cell Reports},

  number       = 9,

  volume       = 13,

  place        = {Netherlands},

  year         = {Tue Dec 01 00:00:00 EST 2015},

  month        = {Tue Dec 01 00:00:00 EST 2015}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Publisher's Version of Record
https://doi.org/10.1016/j.celrep.2015.10.062

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 34 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:

Structural and Dynamic Basis for Low-Affinity, High-Selectivity Binding of L-Glutamine by the Glutamine Riboswitch

Journal Article Ren, Aiming ; Xue, Yi ; Peselis, Alla ; ... - Cell Reports
https://doi.org/10.1016/j.celrep.2015.10.062
Structural Basis of Low-Affinity Nickel Binding to the Nickel-Responsive Transcription Factor NikR from Escherichia coli

Journal Article Phillips, C ; Schreiter, E ; Stultz, C ; ... - Biochemistry

Escherichia coli NikR regulates cellular nickel uptake by binding to the nik operon in the presence of nickel and blocking transcription of genes encoding the nickel uptake transporter. NikR has two binding affinities for the nik operon: a nanomolar dissociation constant with stoichiometric nickel and a picomolar dissociation constant with excess nickel [Bloom, S. L., and Zamble, D. B. (2004) Biochemistry 43, 10029-10038; Chivers, P. T., and Sauer, R. T. (2002) Chem. Biol. 9, 1141-1148]. While it is known that the stoichiometric nickel ions bind at the NikR tetrameric interface [Schreiter, E. R., et al. (2003) Nat. Struct. Biol. 10,more »« less
https://doi.org/10.1021/bi100923j
Short-term desensitization of muscarinic cholinergic receptors in mouse neuroblastoma cells: selective loss of agonist low-affinity and pirenzepine high-affinity binding sites

Journal Article Cioffi, C L ; el-Fakahany, E E - J. Pharmacol. Exp. Ther.; (United States)

The effects of brief incubation with carbamylcholine on subsequent binding of (/sup 3/H)N-methylscopolamine were investigated in mouse neuroblastoma cells (clone N1E-115). This treatment demonstrated that the muscarinic receptors in this neuronal clone can be divided into two types; one which is readily susceptible to regulation by receptor agonists, whereas the other is resistant in this regard. In control cells, both pirenzepine and carbamylcholine interacted with high- and low-affinity subsets of muscarinic receptors. Computer-assisted analysis of the competition between pirenzepine and carbamylcholine with (/sup 3/H)N-methylscopolamine showed that the receptor sites remaining upon desensitization are composed mainly of pirenzepine low-affinity and agonistmore »« less
Structural basis for high substrate-binding affinity and enantioselectivity of 3-quinuclidinone reductase AtQR

Journal Article Hou, Feng ; Miyakawa, Takuya ; Kataoka, Michihiko ; ... - Biochemical and Biophysical Research Communications

Highlights: • Crystal structure of AtQR has been determined at 1.72 Å. • NADH binding induces the formation of substrate binding site. • AtQR possesses a conserved hydrophobic wall for stereospecific binding of substrate. • Additional Glu197 residue is critical to the high binding affinity. - Abstract: (R)-3-Quinuclidinol, a useful compound for the synthesis of various pharmaceuticals, can be enantioselectively produced from 3-quinuclidinone by 3-quinuclidinone reductase. Recently, a novel NADH-dependent 3-quinuclidionone reductase (AtQR) was isolated from Agrobacterium tumefaciens, and showed much higher substrate-binding affinity (>100 fold) than the reported 3-quinuclidionone reductase (RrQR) from Rhodotorula rubra. Here, we report the crystalmore »« less
https://doi.org/10.1016/J.BBRC.2014.03.030
Structural Basis for High-Affinity Her2 Receptor Binding by an Engineered Protein

Journal Article Eigenbrot, C ; Ultsch, M ; Dubnovitsky, A ; ... - Proc.Nat.Acad.Sci.107:15039,2010

Similar Records