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Structural basis of the cooperative activation of type II citrate synthase (HyCS) from Hymenobacter sp. PAMC 26554.
Park, Sun-Ha; Lee, Chang Woo; Bae, Da-Woon; Do, Hackwon; Jeong, Chang-Sook; Hwang, Jisub; Cha, Sun-Shin; Lee, Jun Hyuck.
Afiliación
  • Park SH; Research Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
  • Lee CW; Research Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 21990, Republic of Korea; Department of Polar Sciences, University of Science and Technology, Incheon 21990, Republic of Korea.
  • Bae DW; Department of Chemistry & Nanoscience, Ewha Womans University, Seoul 03760, Republic of Korea.
  • Do H; Research Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
  • Jeong CS; Research Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 21990, Republic of Korea; Department of Polar Sciences, University of Science and Technology, Incheon 21990, Republic of Korea.
  • Hwang J; Research Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 21990, Republic of Korea; Department of Polar Sciences, University of Science and Technology, Incheon 21990, Republic of Korea.
  • Cha SS; Department of Chemistry & Nanoscience, Ewha Womans University, Seoul 03760, Republic of Korea. Electronic address: chajung@ewha.ac.kr.
  • Lee JH; Research Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 21990, Republic of Korea; Department of Polar Sciences, University of Science and Technology, Incheon 21990, Republic of Korea. Electronic address: junhyucklee@kopri.re.kr.
Int J Biol Macromol ; 183: 213-221, 2021 Jul 31.
Article en En | MEDLINE | ID: mdl-33910038
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Citrato (si)-Sintasa / Ácido Cítrico / Bacteroidetes Idioma: En Revista: Int J Biol Macromol Año: 2021 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
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Imprimir
XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Citrato (si)-Sintasa / Ácido Cítrico / Bacteroidetes Idioma: En Revista: Int J Biol Macromol Año: 2021 Tipo del documento: Article Pais de publicación: Países Bajos