1SR3

Solution structure of the heme chaperone CcmE of Escherichia coli

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1SR3 の概要

• エントリーDOI: 10.2210/pdb1sr3/pdb
• 分子名称: APO-CCME (1 entity in total)
• 機能のキーワード: ob fold, beta barrel, flexible c-terminal domain, chaperone
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Single-pass type II membrane protein; Periplasmic side (Potential): P69490
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15349.21

構造登録者

Enggist, E.,Thony-Meyer, L.,Guntert, P.,Pervushin, K. (登録日: 2004-03-22, 公開日: 2004-04-06, 最終更新日: 2024-05-29)

主引用文献

Enggist, E.,Thony-Meyer, L.,Guntert, P.,Pervushin, K.
NMR Structure of the Heme Chaperone Ccme Reveals a Novel Functional Motif
Structure, 10:1551-1557, 2002

PubMed Abstract: The concept of metal chaperones involves transient binding of metallic cofactors by specific proteins for delivery to enzymes in which they function. Metal chaperones thus provide a protective, as well as a transport, function. We report the first structure of a heme chaperone, CcmE, which comprises these two functions. We propose that the covalent attachment of heme to an exposed histidine occurs after heme binding at the surface of a rigid molecule with a flexible C-terminal domain. CcmE belongs to a family of proteins with a specific fold, which all share a function in delivery of specific molecular cargo.

PubMed: 12429096
DOI: 10.1016/S0969-2126(02)00885-7

実験手法

SOLUTION NMR