1QXN

Solution Structure of the 30 kDa Polysulfide-sulfur Transferase Homodimer from Wolinella Succinogenes

Summary for 1QXN

• Entry DOI: 10.2210/pdb1qxn/pdb
• NMR Information: BMRB: 4776
• Descriptor: sulfide dehydrogenase, PENTASULFIDE-SULFUR (2 entities in total)
• Functional Keywords: polysulfide-sulfur transferase, sud, homodimer, transferase
• Biological source: Wolinella succinogenes
• Total number of polymer chains: 2
• Total formula weight: 31036.03

Authors

Lin, Y.J.,Dancea, F.,Loehr, F.,Klimmek, O.,Pfeiffer-Marek, S.,Nilges, M.,Wienk, H.,Kroeger, A.,Rueterjans, H. (deposition date: 2003-09-08, release date: 2004-02-24, Last modification date: 2024-10-30)

Primary citation

Lin, Y.J.,Dancea, F.,Loehr, F.,Klimmek, O.,Pfeiffer-Marek, S.,Nilges, M.,Wienk, H.,Kroeger, A.,Rueterjans, H.
Solution Structure of the 30 kDa Polysulfide-Sulfur Transferase Homodimer from Wolinella succinogenes
Biochemistry, 43:1418-1424, 2004

PubMed Abstract: 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.

PubMed: 14769017
DOI: 10.1021/bi0356597

Experimental method

SOLUTION NMR