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5db5

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'''Unreleased structure'''
 
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The entry 5db5 is ON HOLD until Paper Publication
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==Crystal structure of PLP-bound E. coli SufS (cysteine persulfide intermediate) in space group P21==
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<StructureSection load='5db5' size='340' side='right' caption='[[5db5]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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Authors: Arbing, M.A., Shin, A., Koo, C.W., Medrano-Soto, A., Eisenberg, D.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5db5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DB5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DB5 FirstGlance]. <br>
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Description: Crystal structure of PLP-bound E. coli SufS (cysteine persulfide intermediate) in space group P21
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5db5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5db5 OCA], [http://pdbe.org/5db5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5db5 RCSB], [http://www.ebi.ac.uk/pdbsum/5db5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5db5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/SUFS_ECOLI SUFS_ECOLI]] Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.<ref>PMID:10829016</ref> <ref>PMID:12089140</ref> <ref>PMID:11997471</ref> <ref>PMID:12876288</ref> <ref>PMID:12941942</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Arbing, M A]]
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[[Category: Eisenberg, D]]
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[[Category: Koo, C W]]
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[[Category: Medrano-Soto, A]]
[[Category: Shin, A]]
[[Category: Shin, A]]
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[[Category: Koo, C.W]]
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[[Category: Cysteine desulfurase]]
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[[Category: Medrano-Soto, A]]
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[[Category: Lyase]]
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[[Category: Eisenberg, D]]
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[[Category: Nifs protein family]]
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[[Category: Arbing, M.A]]
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[[Category: Protein binding]]
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[[Category: Transferase]]

Revision as of 06:49, 10 September 2016

Crystal structure of PLP-bound E. coli SufS (cysteine persulfide intermediate) in space group P21

5db5, resolution 2.75Å

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