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7kmy

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'''Unreleased structure'''
 
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The entry 7kmy is ON HOLD
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==Structure of Mtb Lpd bound to 010705==
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<StructureSection load='7kmy' size='340' side='right'caption='[[7kmy]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7kmy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KMY 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]] 2.21&#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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=WPM:N~2~-methyl-N~2~-[(5-methyl-1H-indazol-7-yl)sulfonyl]-N-(1-methyl-2-oxo-1,2-dihydropyridin-4-yl)glycinamide'>WPM</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7kmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kmy OCA], [https://pdbe.org/7kmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kmy RCSB], [https://www.ebi.ac.uk/pdbsum/7kmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kmy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DLDH_MYCTU DLDH_MYCTU] Lipoamide dehydrogenase is an essential component of the alpha-ketoacid dehydrogenase complexes, namely the pyruvate dehydrogenase (PDH) complex, the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, and likely also the 2-oxoglutarate dehydrogenase (ODH) complex. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the complexes. Is also able to catalyze the transhydrogenation of NADH and thio-NAD(+) in the absence of D,L-lipoamide, and the NADH-dependent reduction of quinones in vitro.<ref>PMID:11560483</ref> <ref>PMID:11799204</ref> <ref>PMID:16045627</ref> <ref>PMID:21238944</ref> <ref>PMID:16093239</ref> Together with AhpC, AhpD and DlaT, Lpd constitutes an NADH-dependent peroxidase active against hydrogen and alkyl peroxides as well as serving as a peroxynitrite reductase, thus protecting the bacterium against reactive nitrogen intermediates and oxidative stress generated by the host immune system.<ref>PMID:11560483</ref> <ref>PMID:11799204</ref> <ref>PMID:16045627</ref> <ref>PMID:21238944</ref> <ref>PMID:16093239</ref> Appears to be essential for Mtb pathogenesis.<ref>PMID:11560483</ref> <ref>PMID:11799204</ref> <ref>PMID:16045627</ref> <ref>PMID:21238944</ref> <ref>PMID:16093239</ref>
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Authors:
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==See Also==
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*[[Dihydrolipoamide dehydrogenase|Dihydrolipoamide dehydrogenase]]
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Description:
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Lima CD]]

Current revision

Structure of Mtb Lpd bound to 010705

PDB ID 7kmy

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