1elq

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[[Image:1elq.png|left|200px]]
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==CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES==
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<StructureSection load='1elq' size='340' side='right' caption='[[1elq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1elq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp._pcc_6714 Synechocystis sp. pcc 6714]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ELQ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1elu|1elu]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1elq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1elq RCSB], [http://www.ebi.ac.uk/pdbsum/1elq PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/el/1elq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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FeS clusters are versatile cofactors of a variety of proteins, but the mechanisms of their biosynthesis are still unknown. The cystine C-S lyase from Synechocystis has been identified as a participant in ferredoxin FeS cluster formation. Herein, we report on the crystal structure of the lyase and of a complex with the reaction products of cystine cleavage at 1.8- and 1.55-A resolution, respectively. The sulfur-containing product was unequivocally identified as cysteine persulfide. The reactive persulfide group is fixed by a hydrogen bond to His-114 in the center of a hydrophobic pocket and is thereby shielded from the solvent. Binding and stabilization of the cysteine persulfide represent an alternative to the generation of a protein-bound persulfide by NifS-like proteins and point to the general importance of persulfidic compounds for FeS cluster assembly.
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{{STRUCTURE_1elq| PDB=1elq | SCENE= }}
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Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis.,Clausen T, Kaiser JT, Steegborn C, Huber R, Kessler D Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):3856-61. PMID:10760256<ref>PMID:10760256</ref>
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===CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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==About this Structure==
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<references/>
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[[1elq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp._pcc_6714 Synechocystis sp. pcc 6714]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELQ OCA].
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__TOC__
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:010760256</ref><references group="xtra"/>
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[[Category: Synechocystis sp. pcc 6714]]
[[Category: Synechocystis sp. pcc 6714]]
[[Category: Clausen, T.]]
[[Category: Clausen, T.]]

Revision as of 11:27, 24 September 2014

CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES

1elq, resolution 1.80Å

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