1kmk: Difference between revisions

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[[Image:1kmk.png|left|200px]]


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==E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).==
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<StructureSection load='1kmk' size='340' side='right'caption='[[1kmk]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1kmk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KMK FirstGlance]. <br>
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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]] 2.2&#8491;</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=CSZ:S-SELANYL+CYSTEINE'>CSZ</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SEC:SELENOCYSTEINE'>SEC</scene></td></tr>
{{STRUCTURE_1kmk|  PDB=1kmk  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kmk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmk OCA], [https://pdbe.org/1kmk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kmk RCSB], [https://www.ebi.ac.uk/pdbsum/1kmk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kmk ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1kmk TOPSAN]</span></td></tr>
</table>
== Function ==
[https://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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/1kmk_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1kmk ConSurf].
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== Publication Abstract from PubMed ==
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.


===E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).===
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1kmk" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_11853669}}, adds the Publication Abstract to the page
*[[Selenocysteine lyase|Selenocysteine lyase]]
(as it appears on PubMed at http://www.pubmed.gov), where 11853669 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_11853669}}
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</StructureSection>
==About this Structure==
1KMK is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMK OCA].
 
==Reference==
Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1., Bernier-Villamor V, Sampson DA, Matunis MJ, Lima CD, Cell. 2002 Feb 8;108(3):345-56. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11853669 11853669]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Selenocysteine lyase]]
[[Category: Large Structures]]
[[Category: Burley, S K.]]
[[Category: Burley SK]]
[[Category: Lima, C D.]]
[[Category: Lima CD]]
[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
[[Category: New york structural genomix research consortium]]
[[Category: Nifs selenocysteine cysteine persulfide perselenide xray]]
[[Category: Nysgxrc]]
[[Category: Protein structure initiative]]
[[Category: Psi]]
[[Category: Structural genomic]]
 
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