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==CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES==
==CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES==
<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 ==
<table><tr><td colspan='2'>[[1elq]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ELQ FirstGlance]. <br>
<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>
</td></tr><tr id='ligand'><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></td></tr>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1elu|1elu]]</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>
<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=1elq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elq OCA], [http://pdbe.org/1elq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1elq RCSB], [http://www.ebi.ac.uk/pdbsum/1elq PDBsum], [http://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>
== Function ==
[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>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1elq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Clausen, T]]
[[Category: Large Structures]]
[[Category: Huber, R]]
[[Category: Synechocystis sp. PCC 6714]]
[[Category: Kaiser, J T]]
[[Category: Clausen T]]
[[Category: Kessler, D]]
[[Category: Huber R]]
[[Category: Steegborn, C]]
[[Category: Kaiser JT]]
[[Category: Fes cluster biosynthesis]]
[[Category: Kessler D]]
[[Category: Lyase]]
[[Category: Steegborn C]]
[[Category: Nif]]
[[Category: Pyridoxal 5'-phosphate]]
[[Category: Thiocysteine]]

Latest revision as of 13:04, 20 March 2024

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

Structural highlights

1elq is a 2 chain structure with sequence from Synechocystis sp. PCC 6714. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9ZHG9_SYNY4

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1elq, resolution 1.80Å

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OCA
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