1kmj

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==E. coli NifS/CsdB protein at 2.0A with the cysteine persulfide intermediate (residue CSS).==
==E. coli NifS/CsdB protein at 2.0A with the cysteine persulfide intermediate (residue CSS).==
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<StructureSection load='1kmj' size='340' side='right'caption='[[1kmj]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='1kmj' size='340' side='right'caption='[[1kmj]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1kmj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KMJ FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KMJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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</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=1kmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmj OCA], [https://pdbe.org/1kmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kmj RCSB], [https://www.ebi.ac.uk/pdbsum/1kmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kmj ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1kmj TOPSAN]</span></td></tr>
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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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jf9|1jf9]]</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Selenocysteine_lyase Selenocysteine lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.16 4.4.1.16] </span></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=1kmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmj OCA], [http://pdbe.org/1kmj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kmj RCSB], [http://www.ebi.ac.uk/pdbsum/1kmj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kmj ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1kmj TOPSAN]</span></td></tr>
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</table>
</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>
 
== 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=1kmj 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=1kmj 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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The Escherichia coli NifS CsdB protein is a member of the homodimeric pyridoxal 5'-phosphate (PLP)-dependent family of enzymes. These enzymes are capable of decomposing cysteine or selenocysteine into L-alanine and sulfur or selenium, respectively. E. coli NifS CsdB has a high specificity for L-selenocysteine in comparison to l-cysteine, suggesting a role for this enzyme is selenium metabolism. The 2.0 A crystal structure of E. coli NifS CsdB reveals a high-resolution view of the active site of this enzyme in apo-, persulfide, perselenide, and selenocysteine-bound intermediates, suggesting a mechanism for the stabilization of the enzyme persulfide and perselenide intermediates during catalysis, a necessary intermediate in the formation of sulfur and selenium containing metabolites.
 
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Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation.,Lima CD J Mol Biol. 2002 Feb 1;315(5):1199-208. PMID:11827487<ref>PMID:11827487</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 1kmj" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Selenocysteine lyase|Selenocysteine lyase]]
*[[Selenocysteine lyase|Selenocysteine lyase]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Selenocysteine lyase]]
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[[Category: Burley SK]]
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[[Category: Burley, S K]]
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[[Category: Lima CD]]
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[[Category: Lima, C D]]
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[[Category: Structural genomic]]
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[[Category: Lyase]]
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[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
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[[Category: Persulfide perselenide nifs pyridoxal phosphate]]
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[[Category: PSI, Protein structure initiative]]
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Revision as of 08:48, 21 April 2021

E. coli NifS/CsdB protein at 2.0A with the cysteine persulfide intermediate (residue CSS).

PDB ID 1kmj

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