4BZ4

CorA is a surface-associated copper-binding protein important in Methylomicrobium album BG8 copper acquisition

4BZ4 の概要

• エントリーDOI: 10.2210/pdb4bz4/pdb
• 分子名称: COPPER-REPRESSIBLE POLYPEPTIDE, COPPER (I) ION, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: copper-binding protein, copper acquisition, methanotroph
• 由来する生物種: METHYLOMICROBIUM ALBUM BG8
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 155368.07

構造登録者

Johnson, K.A.,Ve, T.,Pedersen, R.B.,Lillehaug, J.R.,Jensen, H.B.,Helland, R.,Karlsen, O.A. (登録日: 2013-07-24, 公開日: 2014-02-19, 最終更新日: 2024-11-13)

主引用文献

Johnson, K.A.,Ve, T.,Larsen, O.,Pedersen, R.B.,Lillehaug, J.R.,Jensen, H.B.,Helland, R.,Karlsen, O.A.
Cora is a Copper Repressible Surface-Associated Copper(I)-Binding Protein Produced in Methylomicrobium Album Bg8.
Plos One, 9:87750-, 2014

PubMed Abstract: CorA is a copper repressible protein previously identified in the methanotrophic bacterium Methylomicrobium album BG8. In this work, we demonstrate that CorA is located on the cell surface and binds one copper ion per protein molecule, which, based on X-ray Absorption Near Edge Structure analysis, is in the reduced state (Cu(I)). The structure of endogenously expressed CorA was solved using X-ray crystallography. The 1.6 Å three-dimensional structure confirmed the binding of copper and revealed that the copper atom was coordinated in a mononuclear binding site defined by two histidines, one water molecule, and the tryptophan metabolite, kynurenine. This arrangement of the copper-binding site is similar to that of its homologous protein MopE* from Metylococcus capsulatus Bath, confirming the importance of kynurenine for copper binding in these proteins. Our findings show that CorA has an overall fold similar to MopE, including the unique copper(I)-binding site and most of the secondary structure elements. We suggest that CorA plays a role in the M. album BG8 copper acquisition.

PubMed: 24498370
DOI: 10.1371/JOURNAL.PONE.0087750

実験手法

X-RAY DIFFRACTION (1.6 Å)