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Solution structure of the 30 kDa polysulfide-sulfur transferase homodimer from Wolinella succinogenes
- Source :
- Biochemistry. 43(6)
- Publication Year :
- 2004
-
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.
- Subjects :
- inorganic chemicals
Protein Conformation
Dimer
Molecular Sequence Data
Sulfides
Crystallography, X-Ray
Biochemistry
Protein Structure, Secondary
Residue (chemistry)
chemistry.chemical_compound
Structure-Activity Relationship
Transferase
Amino Acid Sequence
Nuclear Magnetic Resonance, Biomolecular
chemistry.chemical_classification
Binding Sites
biology
Chemistry
Active site
Electron acceptor
Wolinella
Molecular Weight
Solutions
Crystallography
Covalent bond
Residual dipolar coupling
Sulfurtransferases
biology.protein
Polysulfide reductase
Oxidoreductases
Dimerization
Sequence Alignment
Sulfur
Subjects
Details
- ISSN :
- 00062960
- Volume :
- 43
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Biochemistry
- Accession number :
- edsair.doi.dedup.....bf64110ecb840c56c788a526d5664ef2