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Crystal structure of the YffB protein from Pseudomonas aeruginosa suggests a glutathione-dependent thiol reductase function
Authors:Alexey?Teplyakov  author-information"  >  author-information__contact u-icon-before"  >  mailto:teplyako@umbi.umd.edu"   title="  teplyako@umbi.umd.edu"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author,Sadhana?Pullalarevu,Galina?Obmolova,Victoria?Doseeva,Andrey?Galkin,Osnat?Herzberg,Miroslawa?Dauter,Zbigniew?Dauter,Gary?L?Gilliland  author-information"  >  author-information__contact u-icon-before"  >  mailto:gilliland@nist.gov"   title="  gilliland@nist.gov"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author
Affiliation:(1) Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, MD, 20850, U.S.A;(2) National Cancer Institute, Brookhaven National Laboratory, Building 725A-X9, Upton, NY, 11973, U.S.A
Abstract:

Background  

The yffB (PA3664) gene of Pseudomonas aeruginosa encodes an uncharacterized protein of 13 kDa molecular weight with a marginal sequence similarity to arsenate reductase from Escherichia coli. The crystal structure determination of YffB was undertaken as part of a structural genomics effort in order to assist with the functional assignment of the protein.
Keywords:
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