1qxn

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[[Image:1qxn.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qxn OCA], [http://www.ebi.ac.uk/pdbsum/1qxn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qxn RCSB]</span>
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'''Solution Structure of the 30 kDa Polysulfide-sulfur Transferase Homodimer from Wolinella Succinogenes'''
'''Solution Structure of the 30 kDa Polysulfide-sulfur Transferase Homodimer from Wolinella Succinogenes'''
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[[Category: Rueterjans, H.]]
[[Category: Rueterjans, H.]]
[[Category: Wienk, H.]]
[[Category: Wienk, H.]]
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[[Category: homodimer]]
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[[Category: Homodimer]]
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[[Category: polysulfide-sulfur transferase]]
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[[Category: Polysulfide-sulfur transferase]]
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[[Category: sud]]
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[[Category: Sud]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:49:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:20:24 2008''
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Revision as of 03:49, 3 May 2008

Template:STRUCTURE 1qxn

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. 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 May 3 06:49:30 2008

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