1YRH

Crystal Structure Of Trp Repressor Binding Protein Wrba in complex with FMN

Summary for 1YRH

• Entry DOI: 10.2210/pdb1yrh/pdb
• Related: 1YDG
• Descriptor: trp repressor binding protein WrbA, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: alpha-beta twisted open sheet, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, protein binding
• Biological source: Deinococcus radiodurans
• Total number of polymer chains: 8
• Total formula weight: 186856.24

Authors

Gorman, J.,Shapiro, L.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2005-02-03, release date: 2005-02-15, Last modification date: 2021-02-03)

Primary citation

Gorman, J.,Shapiro, L.
Crystal structures of the tryptophan repressor binding protein WrbA and complexes with flavin mononucleotide.
Protein Sci., 14:3004-3012, 2005

PubMed Abstract: 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.

PubMed: 16322580
DOI: 10.1110/ps.051680805

Experimental method

X-RAY DIFFRACTION (3.11 Å)