DsbA

Motility protein B
Crystal structure of DsbA.[1]
Identifiers
Symbol	motB
Entrez	946402
UniProt	P0AF06
Other data

DSBA oxidoreductase
Identifiers
Symbol	DSBA
Pfam	PF01323
InterPro	IPR001853
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

DSBA oxidoreductase is sub-family of the Thioredoxin family.^[2] The efficient and correct folding of bacterial disulfide bonded proteins in vivo is dependent upon a class of periplasmic oxidoreductase proteins called DsbA, after the Escherichia coli enzyme. The bacterial protein-folding factor DsbA is the most oxidizing of the thioredoxin family. DsbA catalyzes disulfide-bond formation during the folding of secreted proteins. The extremely oxidizing nature of DsbA has been proposed to result from either domain motion or stabilizing active-site interactions in the reduced form. DsbA's highly oxidizing nature is a result of hydrogen bond, electrostatic and helix-dipole interactions that favour the thiolate over the disulfide at the active site.^[3] In the pathogenic bacterium Vibrio cholerae, the DsbA homolog (TcpG) is responsible for the folding, maturation and secretion of virulence factors.

Sequence/ Structure Details:.^[1] The stucture 3L9S has in total 1 chains. Out of these 1 are sequence-unique. The structure of the crystal is composed of 50% helical (9 helices; 97 residues) and 10% beta sheet (6 strands; 21 residues).^[4] The crystal structure of DsbA contains a thioredoxin like fold which includes a central β-strand in the central β-sheet and the insertion of a 65 residue helical domain. These insertions are common within the thioredoxin family.

References

1. ^ ^{a b} PDB 3L9S; "RCSB Protein Data Bank - Structure Summary for 3L9S - Crystal structure of". http://www.pdb.org/pdb/explore/remediatedSequence.do?structureId=3L9S. 
2. ^ Hu SH, Peek JA, Rattigan E, Taylor RK, Martin JL (1997). "Structure of TcpG, the DsbA protein folding catalyst

   from Vibrio cholerae". J. Mol. Biol. 268 (1): 137–146. doi:10.1006/jmbi.1997.0940. PMID 9149147. 

3. ^ Bardwell JC, Martin JL, Guddat LW (1998). "Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization". Structure 6 (6): 757–767. PMID 9655827. 
4. ^ Horwich, Arthur (2002). Advances in protein chemistry. Academic Press. pp. 284–287. http://books.google.com/books?id=3ipKFrFpxD4C&lpg=PA285&ots=DzSLZDei_o&dq=motility%20protein%20dsba&pg=PR4#v=onepage&q=motility%20protein%20dsba&f=false. 

This article includes text from the public domain Pfam and InterPro IPR001853