3sx2

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<StructureSection load='3sx2' size='340' side='right'caption='[[3sx2]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='3sx2' size='340' side='right'caption='[[3sx2]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sx2]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycpa Mycpa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SX2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sx2]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_avium_subsp._paratuberculosis_K-10 Mycobacterium avium subsp. paratuberculosis K-10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SX2 FirstGlance]. <br>
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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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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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]] 1.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAP_2861 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262316 MYCPA])</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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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=3sx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sx2 OCA], [https://pdbe.org/3sx2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sx2 RCSB], [https://www.ebi.ac.uk/pdbsum/3sx2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sx2 ProSAT]</span></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=3sx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sx2 OCA], [https://pdbe.org/3sx2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sx2 RCSB], [https://www.ebi.ac.uk/pdbsum/3sx2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sx2 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q73W00_MYCPA Q73W00_MYCPA]
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During human infection, Mycobacterium tuberculosis (Mtb) survives the normally bacteriocidal phagosome of macrophages. Mtb and related species may be able to combat this harsh acidic environment which contains reactive oxygen species due to the mycobacterial genomes encoding a large number of dehydrogenases. Typically, dehydrogenase cofactor binding sites are open to solvent, which allows NAD/NADH exchange to support multiple turnover. Interestingly, mycobacterial short chain dehydrogenases/reductases (SDRs) within family TIGR03971 contain an insertion at the NAD binding site. Here we present crystal structures of 9 mycobacterial SDRs in which the insertion buries the NAD cofactor except for a small portion of the nicotinamide ring. Line broadening and STD-NMR experiments did not show NAD or NADH exchange on the NMR timescale. STD-NMR demonstrated binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and an external redox partner 2,6-dichloroindophenol (DCIP). Therefore, these SDRs appear to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover. Incidentally, these genes always appear in conjunction with the mftA gene, which encodes the short peptide MftA, and with other genes proposed to convert MftA into the external redox partner mycofactocin.
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Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors.,Haft DH, Pierce PG, Mayclin SJ, Sullivan A, Gardberg AS, Abendroth J, Begley DW, Phan IQ, Staker BL, Myler PJ, Marathias VM, Lorimer DD, Edwards TE Sci Rep. 2017 Jan 25;7:41074. doi: 10.1038/srep41074. PMID:28120876<ref>PMID:28120876</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3sx2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Mycpa]]
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[[Category: Mycobacterium avium subsp. paratuberculosis K-10]]
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[[Category: Structural genomic]]
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[[Category: Mycobacerium paratuberculosis]]
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[[Category: Oxidoreductase]]
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[[Category: Ssgcid]]
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Current revision

Crystal structure of a putative 3-ketoacyl-(acyl-carrier-protein) reductase from Mycobacterium paratuberculosis in complex with NAD

PDB ID 3sx2

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