1MAT

STRUCTURE OF THE COBALT-DEPENDENT METHIONINE AMINOPEPTIDASE FROM ESCHERICHIA COLI: A NEW TYPE OF PROTEOLYTIC ENZYME

1MAT の概要

• エントリーDOI: 10.2210/pdb1mat/pdb
• 分子名称: METHIONYL AMINOPEPTIDASE, COBALT (II) ION (3 entities in total)
• 機能のキーワード: hydrolase(alpha-aminoacylpeptide)
• 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: 29488.70

構造登録者

Roderick, S.L.,Matthews, B.W. (登録日: 1992-12-02, 公開日: 1994-01-31, 最終更新日: 2024-02-14)

主引用文献

Roderick, S.L.,Matthews, B.W.
Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme.
Biochemistry, 32:3907-3912, 1993

PubMed Abstract: The X-ray structure of Escherichia coli methionine aminopeptidase (MAP) has been determined to 2.4-A resolution and refined to a crystallographic R-factor of 18.2%. The fold is novel and displays internal pseudo-2-fold symmetry which structurally relates the first and second halves of the polypeptide chain. The topology consists of a central antiparallel beta-sheet covered on one side by two pairs of alpha-helices and by a C-terminal loop. The other face of the beta-sheet, together with some irregular loops, forms the active site, which contains two cobalt ions 2.9 A apart. These metal ions are liganded by the side chains of Asp 97, Asp 108, Glu 204, Glu 235, and His 171 with approximate octahedral coordination. In terms of both the novel backbone fold and the constitution of the active site, MAP appears to represent a new class of proteolytic enzyme.

PubMed: 8471602
DOI: 10.1021/bi00066a009

実験手法

X-RAY DIFFRACTION (2.4 Å)