1qxn
From Proteopedia
(New page: 200px<br /><applet load="1qxn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qxn" /> '''Solution Structure of the 30 kDa Polysulfide...) |
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| - | [[Image:1qxn.gif|left|200px]]<br /><applet load="1qxn" size=" | + | [[Image:1qxn.gif|left|200px]]<br /><applet load="1qxn" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution Structure of the 30 kDa Polysulfide-sulfur Transferase Homodimer from Wolinella Succinogenes'''<br /> | '''Solution Structure of the 30 kDa Polysulfide-sulfur Transferase Homodimer from Wolinella Succinogenes'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The periplasmic polysulfide-sulfur transferase (Sud) protein encoded by | + | 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== | ==About this Structure== | ||
| - | 1QXN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes] with PS5 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1QXN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes] with <scene name='pdbligand=PS5:'>PS5</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Klimmek, O.]] | [[Category: Klimmek, O.]] | ||
[[Category: Kroeger, A.]] | [[Category: Kroeger, A.]] | ||
| - | [[Category: Lin, Y | + | [[Category: Lin, Y J.]] |
[[Category: Loehr, F.]] | [[Category: Loehr, F.]] | ||
[[Category: Nilges, M.]] | [[Category: Nilges, M.]] | ||
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[[Category: sud]] | [[Category: sud]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:48 2008'' |
Revision as of 12:44, 21 February 2008
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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 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
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