YodA from Escherichia coli is a metal-binding, lipocalin-like protein

被引:50
作者
David, G
Blondeau, K
Schiltz, M
Penel, S
Lewit-Bentley, A
机构
[1] CNRS, CEA, MdR, Lab Utilisat Rayonnement Electromagnet, F-91898 Orsay, France
[2] Ctr Sci Paris Sud, Inst Genet & Microbiol, F-91405 Orsay, France
关键词
D O I
10.1074/jbc.M304484200
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
We have determined the crystal structure of YodA, an Escherichia coli protein of unknown function. YodA had been identified under conditions of cadmium stress, and we confirm that it binds metals such as cadmium and zinc. We have also found nickel bound in one of the crystal forms. YodA is composed of two domains: a main lipocalin/calycin-like domain and a helical domain. The principal metal-binding site lies on one side of the calycin domain, thus making YodA the first metal-binding lipocalin known. Our experiments suggest that YodA expression may be part of a more general stress response. From sequence analogy with the C-terminal domain of a metal-binding receptor of a member of bacterial ATP-binding cassette transporters, we propose a three-dimensional model for this receptor and suggest that YodA may have a receptor-type partner in E. coli.
引用
收藏
页码:43728 / 43735
页数:8
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