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| - | | + | #REDIRECT [[6i2q]] This PDB entry is obsolete and replaced by 6i2q |
| - | ==CRYSTAL STRUCTURE OF MYCOBACTERIUM SMEGMATIS ALPHA-KETOGLUTARATE DECARBOXYLASE IN COMPLEX WITH GARA==
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| - | <StructureSection load='2xt9' size='340' side='right' caption='[[2xt9]], [[Resolution|resolution]] 2.20Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[2xt9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XT9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XT9 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
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| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yic|2yic]], [[2y0p|2y0p]], [[2xta|2xta]], [[2yid|2yid]], [[2xt6|2xt6]]</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/2-oxoglutarate_decarboxylase 2-oxoglutarate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.71 4.1.1.71] </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=2xt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xt9 OCA], [http://pdbe.org/2xt9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xt9 RCSB], [http://www.ebi.ac.uk/pdbsum/2xt9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xt9 ProSAT]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/KGD_MYCS2 KGD_MYCS2]] Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle.<ref>PMID:19019160</ref> <ref>PMID:21867916</ref>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: 2-oxoglutarate decarboxylase]]
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| - | [[Category: Mycs2]]
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| - | [[Category: Alzari, P M]]
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| - | [[Category: Bellinzoni, M]]
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| - | [[Category: Hare, H M.O]]
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| - | [[Category: Wagner, T]]
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| - | [[Category: Wehenkel, A M]]
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| - | [[Category: Kdh]]
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| - | [[Category: Kgd]]
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| - | [[Category: Lyase-signaling protein complex]]
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