Allosteric Determinants in High Temperature Requirement A Enzymes Are Conserved and Regulate the Population of Active Conformations-Reference-Cited by-同舟云学术

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Allosteric Determinants in High Temperature Requirement A Enzymes Are Conserved and Regulate the Population of Active Conformations

Published:2023-06-15 Issue:7 Volume:18 Page:1487-1499
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Gupta Arvind Kumar¹,Singh Kushal²,Patidar Yogesh³,Sharma Ravish³,Sardesai Abhijit A.³,Reddy Govardhan²^ORCID,Gopal Balasubramanian¹^ORCID

Affiliation:

1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India

2. Solid State and Structural Chemistry Unit, Indian Institute of Science, Bangalore 560012, India

3. Centre for DNA Fingerprinting and Diagnostics, Hyderabad 500039, India

Funder

Council of Scientific and Industrial Research, India

Ministry of Electronics and Information technology

Science and Engineering Research Board

Department of Biotechnology, Ministry of Science and Technology, India

Centre for DNA Fingerprinting and Diagnostics

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.2c00921

Reference48 articles.

1. Allostery Is an Intrinsic Property of the Protease Domain of DegS

2. Structural analysis of DegS, a stress sensor of the bacterial periplasm

3. Steric clashes with bound OMP peptides activate the DegS stress-response protease

4. OMP Peptides Modulate the Activity of DegS Protease by Differential Binding to Active and Inactive Conformations

5. OMP Peptides Activate the DegS Stress-Sensor Protease by a Relief of Inhibition Mechanism

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1. Allosteric activation unveils protein-mass modulation of ATP phosphoribosyltransferase product release;Communications Chemistry;2024-04-06

2. Exploring transmembrane allostery in the MexB: DB08385 variant as a promising inhibitor-like candidate against Pseudomonas aeruginosa antibiotic resistance: a computational study;Physical Chemistry Chemical Physics;2024

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