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3l60
From Proteopedia
(Difference between revisions)
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==Crystal structure of branched-chain alpha-keto acid dehydrogenase subunit e2 from mycobacterium tuberculosis== | ==Crystal structure of branched-chain alpha-keto acid dehydrogenase subunit e2 from mycobacterium tuberculosis== | ||
<StructureSection load='3l60' size='340' side='right' caption='[[3l60]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3l60' size='340' side='right' caption='[[3l60]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3l60]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3l60]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L60 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pdhC, Rv2495c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pdhC, Rv2495c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr> |
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></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=3l60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l60 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l60 RCSB], [http://www.ebi.ac.uk/pdbsum/3l60 PDBsum]</span></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=3l60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l60 OCA], [http://pdbe.org/3l60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l60 RCSB], [http://www.ebi.ac.uk/pdbsum/3l60 PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/BKDC_MYCTU BKDC_MYCTU]] Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2).<ref>PMID:21238944</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=3l60 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Dihydrolipoyllysine-residue acetyltransferase]] | [[Category: Dihydrolipoyllysine-residue acetyltransferase]] | ||
| - | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Almo, S C]] | [[Category: Almo, S C]] | ||
| - | [[Category: | + | [[Category: Bonanno, J B]] |
[[Category: Burley, S K]] | [[Category: Burley, S K]] | ||
[[Category: Freeman, J]] | [[Category: Freeman, J]] | ||
Revision as of 20:01, 9 March 2016
Crystal structure of branched-chain alpha-keto acid dehydrogenase subunit e2 from mycobacterium tuberculosis
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Categories: Dihydrolipoyllysine-residue acetyltransferase | Almo, S C | Bonanno, J B | Burley, S K | Freeman, J | Structural genomic | Patskovsky, Y | Sauder, J M | Toro, R | Zencheck, W D | Dehydrogenase | NYSGXRC, New York SGX Research Center for Structural Genomics | Oxidoreductase | PSI, Protein structure initiative
