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| | <StructureSection load='1z6k' size='340' side='right'caption='[[1z6k]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1z6k' size='340' side='right'caption='[[1z6k]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1z6k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z6K OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z6K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1z6k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z6K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z6K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</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]] 2.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1u5h|1u5h]], [[1sgj|1sgj]]</div></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=1z6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z6k OCA], [https://pdbe.org/1z6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z6k RCSB], [https://www.ebi.ac.uk/pdbsum/1z6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z6k ProSAT], [https://www.topsan.org/Proteins/TBSGC/1z6k TOPSAN]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv2498c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Citrate_(pro-3S)-lyase Citrate (pro-3S)-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.6 4.1.3.6] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1z6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z6k OCA], [http://pdbe.org/1z6k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z6k RCSB], [http://www.ebi.ac.uk/pdbsum/1z6k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z6k ProSAT], [http://www.topsan.org/Proteins/TBSGC/1z6k TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CITEL_MYCTU CITEL_MYCTU]] May play a role in fatty acid biosynthesis (Potential). | + | [https://www.uniprot.org/uniprot/CITEL_MYCTU CITEL_MYCTU] May play a role in fatty acid biosynthesis (Potential). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Bowers, P M]] | + | [[Category: Bowers PM]] |
| - | [[Category: Eisenberg, D]] | + | [[Category: Eisenberg D]] |
| - | [[Category: Goulding, C W]] | + | [[Category: Goulding CW]] |
| - | [[Category: Kim, C Y]] | + | [[Category: Kim CY]] |
| - | [[Category: Lekin, T]] | + | [[Category: Lekin T]] |
| - | [[Category: Segelke, B]] | + | [[Category: Segelke B]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Terwilliger TC]] |
| - | [[Category: Terwilliger, T C]] | + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Tbsgc]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
CITEL_MYCTU May play a role in fatty acid biosynthesis (Potential).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Fatty acid biosynthesis is essential for the survival of Mycobacterium tuberculosis and acetyl-coenzyme A (acetyl-CoA) is an essential precursor in this pathway. We have determined the 3-D crystal structure of M. tuberculosis citrate lyase beta-subunit (CitE), which as annotated should cleave protein bound citryl-CoA to oxaloacetate and a protein-bound CoA derivative. The CitE structure has the (beta/alpha)(8) TIM barrel fold with an additional alpha-helix, and is trimeric. We have determined the ternary complex bound with oxaloacetate and magnesium, revealing some of the conserved residues involved in catalysis. While the bacterial citrate lyase is a complex with three subunits, the M. tuberculosis genome does not contain the alpha and gamma subunits of this complex, implying that M. tuberculosis CitE acts differently from other bacterial CitE proteins. The analysis of gene clusters containing the CitE protein from 168 fully sequenced organisms has led us to identify a grouping of functionally related genes preserved in M. tuberculosis, Rattus norvegicus, Homo sapiens, and Mus musculus. We propose a novel enzymatic function for M. tuberculosis CitE in fatty acid biosynthesis that is analogous to bacterial citrate lyase but producing acetyl-CoA rather than a protein-bound CoA derivative.
The structure and computational analysis of Mycobacterium tuberculosis protein CitE suggest a novel enzymatic function.,Goulding CW, Bowers PM, Segelke B, Lekin T, Kim CY, Terwilliger TC, Eisenberg D J Mol Biol. 2007 Jan 12;365(2):275-83. Epub 2006 Oct 3. PMID:17064730[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goulding CW, Bowers PM, Segelke B, Lekin T, Kim CY, Terwilliger TC, Eisenberg D. The structure and computational analysis of Mycobacterium tuberculosis protein CitE suggest a novel enzymatic function. J Mol Biol. 2007 Jan 12;365(2):275-83. Epub 2006 Oct 3. PMID:17064730 doi:http://dx.doi.org/10.1016/j.jmb.2006.09.086
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