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  4. YodA from Escherichia coli is a Metal-binding, Lipocalin-like Protein
 
research article

YodA from Escherichia coli is a Metal-binding, Lipocalin-like Protein

David, G.
•
Blondeau, K.
•
Schiltz, M.  
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2003
Journal of Biological Chemistry

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.

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Type
research article
DOI
10.1074/jbc.M304484200
Author(s)
David, G.
Blondeau, K.
Schiltz, M.  
Penel, S.
Lewit-Bentley, A.
Date Issued

2003

Published in
Journal of Biological Chemistry
Volume

278

Issue

44

Start page

43728

End page

43735

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LCR  
Available on Infoscience
March 29, 2006
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/229019
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