1qxn
From Proteopedia
|
Solution Structure of the 30 kDa Polysulfide-sulfur Transferase Homodimer from Wolinella Succinogenes
Overview
The periplasmic polysulfide-sulfur transferase (Sud) protein encoded by, Wolinella succinogenes is involved in oxidative phosphorylation with, polysulfide-sulfur as a terminal electron acceptor. The polysulfide-sulfur, is covalently bound to the catalytic Cys residue of the Sud protein and, transferred to the active site of the membranous polysulfide reductase., The solution structure of the homodimeric Sud protein has been determined, using heteronuclear multidimensional NMR techniques. The structure is, based on NOE-derived distance restraints, backbone hydrogen bonds, and, torsion angle restraints as well as residual dipolar coupling restraints, for a refinement of the relative orientation of the monomer units. The, monomer structure consists of a five-stranded parallel beta-sheet, enclosing a hydrophobic core, a two-stranded antiparallel beta-sheet, and, six alpha-helices. The dimer fold is stabilized by hydrophobic residues, and ion pairs found in the contact area between the two monomers. Similar, to rhodanese enzymes, Sud catalyzes the transfer of the polysulfide-sulfur, to the artificial acceptor cyanide. Despite their similar functions and, active sites, the amino acid sequences and structures of these proteins, are quite different.
About this Structure
1QXN is a Single protein structure of sequence from Wolinella succinogenes with PS5 as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of the 30 kDa polysulfide-sulfur transferase homodimer from Wolinella succinogenes., Lin YJ, Dancea F, Lohr F, Klimmek O, Pfeiffer-Marek S, Nilges M, Wienk H, Kroger A, Ruterjans H, Biochemistry. 2004 Feb 17;43(6):1418-24. PMID:14769017
Page seeded by OCA on Sat Nov 24 21:45:07 2007
