3FHK

Crystal structure of APC1446, B.subtilis YphP disulfide isomerase

Summary for 3FHK

• Entry DOI: 10.2210/pdb3fhk/pdb
• Descriptor: UPF0403 protein yphP, SULFATE ION (3 entities in total)
• Functional Keywords: disulfide isomerase, thioredoxin superfamily, cxc motif, structural genomics, surface entropy reduction, ser, psi-2, protein structure initiative, isfi, integrated center for structure and function innovation, unknown function
• Biological source: Bacillus subtilis
• Total number of polymer chains: 4
• Total formula weight: 65349.46

Authors

Derewenda, U.,Boczek, T.,Cooper, D.R.,Yu, M.,Hung, L.,Derewenda, Z.S.,Integrated Center for Structure and Function Innovation (ISFI) (deposition date: 2008-12-09, release date: 2009-09-01, Last modification date: 2024-02-21)

Primary citation

Derewenda, U.,Boczek, T.,Gorres, K.L.,Yu, M.,Hung, L.W.,Cooper, D.,Joachimiak, A.,Raines, R.T.,Derewenda, Z.S.
Structure and function of Bacillus subtilis YphP, a prokaryotic disulfide isomerase with a CXC catalytic motif .
Biochemistry, 48:8664-8671, 2009

PubMed Abstract: The DUF1094 family contains over 100 bacterial proteins, all containing a conserved CXC motif, with unknown function. We solved the crystal structure of the Bacillus subtilis representative, the product of the yphP gene. The protein shows remarkable structural similarity to thioredoxins, with a canonical alphabetaalphabetaalphabetabetaalpha topology, despite low amino acid sequence identity to thioredoxin. The CXC motif is found in the loop immediately downstream of the first beta-strand, in a location equivalent to the CXXC motif of thioredoxins, with the first Cys occupying a position equivalent to the first Cys in canonical thioredoxin. The experimentally determined reduction potential of YphP is E degrees' = -130 mV, significantly higher than that of thioredoxin and consistent with disulfide isomerase activity. Functional assays confirmed that the protein displays a level of isomerase activity that might be biologically significant. We propose a mechanism by which the members of this family catalyze isomerization using the CXC catalytic site.

PubMed: 19653655
DOI: 10.1021/bi900437z

Experimental method

X-RAY DIFFRACTION (2.3 Å)