4m52: Difference between revisions

No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==Structure of Mtb Lpd bound to SL827==
==Structure of Mtb Lpd bound to SL827==
<StructureSection load='4m52' size='340' side='right' caption='[[4m52]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='4m52' size='340' side='right'caption='[[4m52]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4m52]] is a 4 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=4M52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M52 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4m52]] is a 4 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=4M52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M52 FirstGlance]. <br>
</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=M52:N~2~-[(2-AMINO-5-BROMOPYRIDIN-3-YL)SULFONYL]-N-(4-METHOXYPHENYL)-N~2~-METHYLGLYCINAMIDE'>M52</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]] 2.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ii4|3ii4]], [[2a8x|2a8x]]</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=M52:N~2~-[(2-AMINO-5-BROMOPYRIDIN-3-YL)SULFONYL]-N-(4-METHOXYPHENYL)-N~2~-METHYLGLYCINAMIDE'>M52</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpd, LPD RV0462, lpdC, MT0478, MTV038.06, Rv0462 ([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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4m52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m52 OCA], [https://pdbe.org/4m52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m52 RCSB], [https://www.ebi.ac.uk/pdbsum/4m52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m52 ProSAT]</span></td></tr>
<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>
<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=4m52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m52 OCA], [http://pdbe.org/4m52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m52 RCSB], [http://www.ebi.ac.uk/pdbsum/4m52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m52 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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>
[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>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 28: Line 26:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dihydrolipoyl dehydrogenase]]
[[Category: Large Structures]]
[[Category: Lima, C D]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Flavoprotein]]
[[Category: Lima CD]]
[[Category: Glycolysis]]
[[Category: Oxidoreductase]]
[[Category: Redox-active center]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA