1ZWL: Structure Of Wrba From Pseudomonas Aeruginosa In Complex With Fmn

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.
PDB ID: 1ZWLDownload
MMDB ID: 33948
PDB Deposition Date: 2005/6/3
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 2.8  Å
Source Organism:
Similar Structures:
Biological Unit for 1ZWL: tetrameric; determined by author and by software (PISA,PQS)
Molecular Components in 1ZWL
Label Count Molecule
Proteins (4 molecules)
TRP Repressor Binding Protein Wrba(Gene symbol: wrbA)
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB