2a8x

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==Crystal Structure of Lipoamide Dehydrogenase from Mycobacterium tuberculosis==
==Crystal Structure of Lipoamide Dehydrogenase from Mycobacterium tuberculosis==
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<StructureSection load='2a8x' size='340' side='right' caption='[[2a8x]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='2a8x' size='340' side='right'caption='[[2a8x]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2a8x]] is a 2 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=2A8X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A8X FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2a8x]] is a 2 chain structure with sequence from [https://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=2A8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A8X 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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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</td></tr><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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv0462, MT0478, lpdC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv0462, MT0478, lpdC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </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=2a8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a8x OCA], [http://pdbe.org/2a8x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a8x RCSB], [http://www.ebi.ac.uk/pdbsum/2a8x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a8x ProSAT]</span></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=2a8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a8x OCA], [https://pdbe.org/2a8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a8x RCSB], [https://www.ebi.ac.uk/pdbsum/2a8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a8x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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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[[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>
== 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: Dihydrolipoyl dehydrogenase]]
[[Category: Dihydrolipoyl dehydrogenase]]
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[[Category: Large Structures]]
[[Category: Bryk, R]]
[[Category: Bryk, R]]
[[Category: Buglino, J A]]
[[Category: Buglino, J A]]

Revision as of 08:27, 27 January 2021

Crystal Structure of Lipoamide Dehydrogenase from Mycobacterium tuberculosis

PDB ID 2a8x

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