1zwl
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(New page: 200px<br /><applet load="1zwl" size="350" color="white" frame="true" align="right" spinBox="true" caption="1zwl, resolution 2.80Å" /> '''Structure of WrbA fr...)
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Revision as of 15:44, 29 January 2008
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Structure of WrbA from Pseudomonas aeruginosa in complex with FMN
Overview
The tryptophan repressor binding protein WrbA binds to the tryptophan, repressor protein TrpR. Although the biological role of WrbA remains, unclear, it has been proposed to function in enhancing the stability of, TrpR-DNA complexes. Sequence database analysis has identified WrbA as a, founding member of a flavodoxin-like family of proteins. Here we present, crystal structures of WrbA from Deinococcus radiodurans and Pseudomonas, aeruginosa and their complexes with flavin mononucleotide. The protomer, structure is similar to that of previously determined long-chain, flavodoxins; however, each contains a conserved inserted region unique to, the WrbA family. Interestingly, each WrbA protein forms a homotetramer, with 222 symmetry, unique among flavodoxin-like proteins, in which each, protomer binds one flavin mononucleotide cofactor molecule.
About this Structure
1ZWL is a Single protein structure of sequence from Pseudomonas aeruginosa with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of the tryptophan repressor binding protein WrbA and complexes with flavin mononucleotide., Gorman J, Shapiro L, Protein Sci. 2005 Dec;14(12):3004-12. PMID:16322580
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