A novel copper site in a cyanobacterial metallochaperone

被引：24

作者：

Borrelly, GPM

Blindauer, CA

Schmid, R

Butler, CS

Cooper, CE

Harvey, I

Sadler, PJ

Robinson, NJ ^{[1
]}

机构：

[1] Univ Newcastle Upon Tyne, Sch Med, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England

[2] Univ Edinburgh, Sch Chem, Edinburgh EH9 3JJ, Midlothian, Scotland

[3] Univ Edinburgh, Inst Cell Anim & Populat Biol, Edinburgh EH9 3JT, Midlothian, Scotland

[4] Univ Essex, Dept Biol Sci, Colchester CO4 3SQ, Essex, England

[5] Council Cent Lab Res Councils, Daresbury Lab, Warrington WA4 4AD, Cheshire, England

来源：

BIOCHEMICAL JOURNAL | 2004年 / 378卷 / 02期

关键词：

Atx1; copper metallochaperone; Synechocystis PCC6803; thylakoid;

D O I：

10.1042/BJ20031669

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The thylakoid lumen of the cyanobacterium Synechocystis PCC 6803 is supplied with copper via two copper-transporting ATPases and a metallochaperone intermediary. We show that the copper site of this metallochaperone is unusual and consists of two cysteine residues and a histidine imidazole located on structurally dynamic loops. Substitution of this histidine residue enhances bacterial two-hybrid interaction with the cytosolic copper exporter, but not the copper importer, suggesting that the interacting surfaces are distinct, with implications for metal transfer.

引用

页码：293 / 297

页数：5

共 26 条

[1] Solution structure of the Cu(I) and Apo forms of the yeast metallochaperone, Atx1 [J].