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Structural basis of the cooperative activation of type II citrate synthase (HyCS) from Hymenobacter sp. PAMC 26554

Cited 1 time in wos
Cited 2 time in scopus
Title
Structural basis of the cooperative activation of type II citrate synthase (HyCS) from Hymenobacter sp. PAMC 26554
Other Titles
남극 지의류에서 분리한 공생 미생물 (Hymenobacter sp. PAMC 26554) 유래 citrate synthase 효소 (HyCS) 의 구조분석을 통한 활성기작 연구
Authors
Park, Sun-Ha
Lee, Chang Woo
Bae, Da-Woon
Do, Hackwon
Jeong, Chang-Sook
Hwang, Jisub
Cha, Sun-Shin
Lee, Jun Hyuck
Subject
Biochemistry & Molecular BiologyChemistryPolymer Science
Keywords
Crystal structureCitrate synthaseHymenobacter spPAMC 26554Domain movementX-ray crystallography
Issue Date
2021-07-31
Citation
Park, Sun-Ha, et al. 2021. "Structural basis of the cooperative activation of type II citrate synthase (HyCS) from Hymenobacter sp. PAMC 26554". INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 183: 213-221.
Abstract
Citrate synthase (CS) catalyzes the formation of citrate and coenzyme A from acetyl-CoA and oxaloacetate. CS exists in two forms: type I and type II. We determined the citrate-bound crystal structure of type II CS from the Hymenobacter sp. PAMC 26554 bacterium (HyCS; isolated from Antarctic lichen). Citrate molecules bound to a cleft between the large and small domains of HyCS. Structural comparison of HyCS with other type II CSs revealed that type II CSs have a highly conserved flexible hinge region (residues G264-P265 in HyCS), enabling correct positioning of active site residues. Notably, the catalytic His266 residue of HyCS interacted with Trp262 in the inactive (unliganded open) state of other type II CSs, whereas the His266 residue moved to the active site via a small-domain swing motion, interacting with the bound citrate in the closed conformation of HyCS. However, type I CSs lack this tryptophan residue and face-to-edge interactions. Thus, type II CSs might have a unique domain-motion control mechanism enabling a tight allosteric regulation. An activity assay using a W262A mutant showed a Hill coefficient of 2.4; thus, the interaction between Trp262 and His266 was closely related to the positive cooperative ligand binding of type II CS. (c) 2021 Published by Elsevier B.V.
URI
https://repository.kopri.re.kr/handle/201206/12983
DOI
http://dx.doi.org/10.1016/j.ijbiomac.2021.04.141
Type
Article
Station
King Sejong Station
Indexed
SCIE
Appears in Collections  
2020-2020, Application study on the Arctic cold-active enzyme degrading organic carbon compounds (20-20) / Kim, Han-Woo (PN20082)
2021-2021, Development of potential candidates as antibiotics based on polar genetic resources (21-21) / Lee, Jun Hyuck (PM21030)
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