1TXT

Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase

1TXT の概要

• エントリーDOI: 10.2210/pdb1txt/pdb
• 関連するPDBエントリー: 1TVZ
• 分子名称: 3-hydroxy-3-methylglutaryl-CoA synthase, ACETOACETYL-COENZYME A (3 entities in total)
• 機能のキーワード: hmg-coa synthase; hmgs, coenzyme a; thiolase fold; condensing enzyme; cholesterol biosynthesis, lyase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 176712.05

構造登録者

Campobasso, N.,Patel, M.,Wilding, I.E.,Kallender, H.,Rosenberg, M.,Gwynn, M. (登録日: 2004-07-06, 公開日: 2004-08-31, 最終更新日: 2024-11-06)

主引用文献

Campobasso, N.,Patel, M.,Wilding, I.E.,Kallender, H.,Rosenberg, M.,Gwynn, M.
Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase: crystal structure and mechanism
J.Biol.Chem., 279:44883-44888, 2004

PubMed Abstract: 3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase, a member of the family of acyl-condensing enzymes, catalyzes the first committed step in the mevalonate pathway and is a potential target for novel antibiotics and cholesterol-lowering agents. The Staphylococcus aureus mvaS gene product (43.2 kDa) was overexpressed in Escherichia coli, purified to homogeneity, and shown biochemically to be an HMG-CoA synthase. The crystal structure of the full-length enzyme was determined at 2.0-A resolution, representing the first structure of an HMG-CoA synthase from any organism. HMG-CoA synthase forms a homodimer. The monomer, however, contains an important core structure of two similar alpha/beta motifs, a fold that is completely conserved among acyl-condensing enzymes. This common fold provides a scaffold for a catalytic triad made up of Cys, His, and Asn required by these enzymes. In addition, a crystal structure of HMG-CoA synthase with acetoacetyl-CoA was determined at 2.5-A resolution. Together, these structures provide the structural basis for an understanding of the mechanism of HMG-CoA synthase.

PubMed: 15292254
DOI: 10.1074/jbc.M407882200

実験手法

X-RAY DIFFRACTION (2.501 Å)