4I52

scMenB im complex with 1-hydroxy-2-naphthoyl-CoA

4I52 の概要

• エントリーDOI: 10.2210/pdb4i52/pdb
• 関連するPDBエントリー: 4EML
• 分子名称: Naphthoate synthase, 1-hydroxy-2-naphthoyl-CoA, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: crotonase, 1, 4-dihydroxy-2-naphthoyl coenzyme a synthase, lyase
• 由来する生物種: Synechocystis sp.
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 281849.93

構造登録者

Song, H.G.,Sun, Y.R.,Li, J.,Li, Y.,Jiang, M.,Zhou, J.H.,Guo, Z.H. (登録日: 2012-11-28, 公開日: 2013-05-08, 最終更新日: 2023-11-08)

主引用文献

Sun, Y.,Song, H.,Li, J.,Li, Y.,Jiang, M.,Zhou, J.,Guo, Z.
Structural basis of the induced-fit mechanism of 1,4-dihydroxy-2-naphthoyl coenzyme a synthase from the crotonase fold superfamily
Plos One, 8:e63095-e63095, 2013

PubMed Abstract: 1, 4-Dihydroxy-2-naphthoyl coenzyme A (DHNA-CoA) synthase is a typical crotonase fold enzyme with an implicated role of conformational changes in catalysis. We have identified these conformational changes by determining the structures of its Escherichia coli and Synechocystis sp. PCC6803 orthologues in complex with a product analog. The structural changes include the folding of an active-site loop into a β-hairpin and significant reorientation of a helix at the carboxy terminus. Interestingly, a new interface is formed between the ordered loop and the reoriented helix, both of which also form additional interactions with the coenzyme A moiety of the ligand. Site-directed mutation of the amino acid residues involved in these ligand-induced interactions significantly diminishes the enzyme activity. These results suggest a catalytically essential induced-fit that is likely initiated by the enzyme-ligand interactions at the active site.

PubMed: 23658663
DOI: 10.1371/journal.pone.0063095

実験手法

X-RAY DIFFRACTION (2.35 Å)