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< | ==Solution Structure of the 30 kDa Polysulfide-sulfur Transferase Homodimer from Wolinella Succinogenes== | ||
<StructureSection load='1qxn' size='340' side='right'caption='[[1qxn]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qxn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QXN FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PS5:PENTASULFIDE-SULFUR'>PS5</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qxn OCA], [https://pdbe.org/1qxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qxn RCSB], [https://www.ebi.ac.uk/pdbsum/1qxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qxn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q56748_WOLSC Q56748_WOLSC] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qx/1qxn_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qxn ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:14769017</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1qxn" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Wolinella succinogenes]] | [[Category: Wolinella succinogenes]] | ||
[[Category: Dancea | [[Category: Dancea F]] | ||
[[Category: Klimmek | [[Category: Klimmek O]] | ||
[[Category: Kroeger | [[Category: Kroeger A]] | ||
[[Category: Lin | [[Category: Lin YJ]] | ||
[[Category: Loehr | [[Category: Loehr F]] | ||
[[Category: Nilges | [[Category: Nilges M]] | ||
[[Category: Pfeiffer-Marek | [[Category: Pfeiffer-Marek S]] | ||
[[Category: Rueterjans | [[Category: Rueterjans H]] | ||
[[Category: Wienk | [[Category: Wienk H]] | ||
Latest revision as of 10:17, 30 October 2024
Solution Structure of the 30 kDa Polysulfide-sulfur Transferase Homodimer from Wolinella SuccinogenesSolution Structure of the 30 kDa Polysulfide-sulfur Transferase Homodimer from Wolinella Succinogenes
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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