PDBsum entry: 1qxn

Transferase

PDB id: 1qxn

Contents

Protein chains

137 a.a. *

Ligands

PS5 ×2

* Residue conservation analysis

PDB id:

1qxn

Name:

Transferase

Title:

Solution structure of the 30 kda polysulfide-sulfur transferase homodimer from wolinella succinogenes

Structure:

Sulfide dehydrogenase. Chain: a, b. Synonym: sud. Engineered: yes

Source:

Wolinella succinogenes. Organism_taxid: 844. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

10 models

Authors:

Y.J.Lin,F.Dancea,F.Loehr,O.Klimmek,S.Pfeiffer-Marek, M.Nilges,H.Wienk,A.Kroeger,H.Rueterjans

Key ref:

Y.J.Lin et al. (2004). Solution structure of the 30 kDa polysulfide-sulfur transferase homodimer from Wolinella succinogenes. Biochemistry, 43, 1418-1424. PubMed id: 14769017 DOI: 10.1021/bi0356597

Date:

08-Sep-03 Release date: 24-Feb-04

Protein chains

Q56748  (Q56748_WOLSU) -  SULFIDE DEHYDROGENASE (Precursor)

Seq: 149 a.a.

Struc: 137 a.a.

DOI no: 10.1021/bi0356597

Biochemistry 43:1418-1424 (2004)

PubMed id: 14769017

Solution structure of the 30 kDa polysulfide-sulfur transferase homodimer from Wolinella succinogenes.

Y.J.Lin, F.Dancea, F.Löhr, O.Klimmek, S.Pfeiffer-Marek, M.Nilges, H.Wienk, A.Kröger, H.Rüterjans.

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.