Crystal Structures of the Tryptophan Repressor binding Protein WrbA and complexes with Flavin Mononucleotide

Journal Article · Sat Jan 01 04:00:00 EST 2005 · Protein Sci.

DOI:https://doi.org/10.1110/ps.051680805· OSTI ID:913919

Gorman, J; Shapiro, L

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.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 913919
• Report Number(s): BNL--78487-2007-JA
• Journal Information: Protein Sci., Journal Name: Protein Sci. Vol. 14
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
CRYSTAL STRUCTURE
PROTEINS
PSEUDOMONAS
STABILITY
SYMMETRY
TRYPTOPHAN
national synchrotron light source