6ABY

Crystal structure of citrate synthase (Msed_1522) from Metallosphaera sedula in complex with oxaloacetate

6ABY の概要

• エントリーDOI: 10.2210/pdb6aby/pdb
• 分子名称: Citrate synthase, OXALOACETATE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: citrate synthase, metallosphaera sedula, transferase
• 由来する生物種: Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88526.52

構造登録者

Lee, S.-H.,Son, H.-F.,Kim, K.-J. (登録日: 2018-07-24, 公開日: 2019-03-20, 最終更新日: 2023-11-22)

主引用文献

Lee, S.H.,Son, H.F.,Kim, K.J.
Structural insights into the inhibition properties of archaeon citrate synthase from Metallosphaera sedula.
PLoS ONE, 14:e0212807-e0212807, 2019

PubMed Abstract: Metallosphaera sedula is a thermoacidophilic archaeon and has an incomplete TCA/glyoxylate cycle that is used for production of biosynthetic precursors of essential metabolites. Citrate synthase from M. sedula (MsCS) is an enzyme involved in the first step of the incomplete TCA/glyoxylate cycle by converting oxaloacetate and acetyl-CoA into citrate and coenzyme A. To elucidate the inhibition properties of MsCS, we determined its crystal structure at 1.7 Å resolution. Like other Type-I CS, MsCS functions as a dimer and each monomer consists of two distinct domains, a large domain and a small domain. The oxaloacetate binding site locates at the cleft between the two domains, and the active site was more closed upon binding of the oxaloacetate substrate than binding of the citrate product. Interestingly, the inhibition kinetic analysis showed that, unlike other Type-I CSs, MsCS is non-competitively inhibited by NADH. Finally, amino acids and structural comparison of MsCS with other Type-II CSs, which were reported to be non-competitively inhibited by NADH, revealed that MsCS has quite unique NADH binding mode for non-competitive inhibition.

PubMed: 30794680
DOI: 10.1371/journal.pone.0212807

実験手法

X-RAY DIFFRACTION (2 Å)