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1MLA

THE ESCHERICHIA COLI MALONYL-COA:ACYL CARRIER PROTEIN TRANSACYLASE AT 1.5-ANGSTROMS RESOLUTION. CRYSTAL STRUCTURE OF A FATTY ACID SYNTHASE COMPONENT

1MLA の概要
エントリーDOI10.2210/pdb1mla/pdb
分子名称MALONYL-COENZYME A ACYL CARRIER PROTEIN TRANSACYLASE (2 entities in total)
機能のキーワードacyltransferase
由来する生物種Escherichia coli
タンパク質・核酸の鎖数1
化学式量合計32443.08
構造登録者
Serre, L.,Verbree, E.C.,Dauter, Z.,Stuitje, A.R.,Derewenda, Z.S. (登録日: 1995-01-25, 公開日: 1996-03-08, 最終更新日: 2024-02-14)
主引用文献Serre, L.,Verbree, E.C.,Dauter, Z.,Stuitje, A.R.,Derewenda, Z.S.
The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component.
J.Biol.Chem., 270:12961-12964, 1995
Cited by
PubMed Abstract: Endogenous fatty acids are synthesized in all organisms in a pathway catalyzed by the fatty acid synthase complex. In bacteria, where the fatty acids are used primarily for incorporation into components of cell membranes, fatty acid synthase is made up of several independent cytoplasmic enzymes, each catalyzing one specific reaction. The initiation of the elongation step, which extends the length of the growing acyl chain by two carbons, requires the transfer of the malonyl moiety from malonyl-CoA onto the acyl carrier protein. We report here the crystal structure (refined at 1.5-A resolution to an R factor of 0.19) of the malonyl-CoA specific transferase from Escherichia coli. The protein has an alpha/beta type architecture, but its fold is unique. The active site inferred from the location of the catalytic Ser-92 contains a typical nucleophilic elbow as observed in alpha/beta hydrolases. Serine 92 is hydrogen bonded to His-201 in a fashion similar to various serine hydrolases. However, instead of a carboxyl acid typically found in catalytic triads, the main chain carbonyl of Gln-250 serves as a hydrogen bond acceptor in an interaction with His-201. Two other residues, Arg-117 and Glu-11, are also located in the active site, although their function is not clear.
PubMed: 7768883
DOI: 10.1074/jbc.270.22.12961
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.5 Å)
構造検証レポート
Validation report summary of 1mla
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-02に公開中

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