1elq

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Current revision (10:04, 20 March 2024) (edit) (undo)
 
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<StructureSection load='1elq' size='340' side='right'caption='[[1elq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1elq' size='340' side='right'caption='[[1elq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1elq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_5.3a) Aphanocapsa sp. (strain 5.3a)]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1ELQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1elq]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1ELQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1elu|1elu]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=1elq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elq OCA], [https://pdbe.org/1elq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elq RCSB], [https://www.ebi.ac.uk/pdbsum/1elq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elq ProSAT]</span></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=1elq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elq OCA], [https://pdbe.org/1elq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elq RCSB], [https://www.ebi.ac.uk/pdbsum/1elq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elq ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9ZHG9_SYNY4 Q9ZHG9_SYNY4]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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/main_output.php?pdb_ID=1elq ConSurf].
</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=1elq ConSurf].
<div style="clear:both"></div>
<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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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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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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<div class="pdbe-citations 1elq" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Clausen, T]]
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[[Category: Synechocystis sp. PCC 6714]]
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[[Category: Huber, R]]
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[[Category: Clausen T]]
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[[Category: Kaiser, J T]]
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[[Category: Huber R]]
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[[Category: Kessler, D]]
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[[Category: Kaiser JT]]
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[[Category: Steegborn, C]]
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[[Category: Kessler D]]
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[[Category: Fes cluster biosynthesis]]
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[[Category: Steegborn C]]
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[[Category: Lyase]]
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[[Category: Nif]]
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[[Category: Pyridoxal 5'-phosphate]]
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[[Category: Thiocysteine]]
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Current revision

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

PDB ID 1elq

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