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3pxx

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Crystal structure of carveol dehydrogenase from Mycobacterium avium bound to nicotinamide adenine dinucleotide

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Retrieved from "http://52.214.119.220/wiki/index.php/3pxx"

Categories: Large Structures | Mycobacterium avium 104

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 <StructureSection load='3pxx' size='340' side='right'caption='[[3pxx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3pxx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Myca1 Myca1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3pxx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_avium_104 Mycobacterium avium 104]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAV_2598 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243243 MYCA1])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/(+)-trans-carveol_dehydrogenase (+)-trans-carveol dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.275 1.1.1.275] </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=3pxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pxx OCA], [https://pdbe.org/3pxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pxx RCSB], [https://www.ebi.ac.uk/pdbsum/3pxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pxx ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/A0A0H2ZV91_MYCA1 A0A0H2ZV91_MYCA1]
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3pxx" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Myca1]]
+[[Category: Mycobacterium avium 104]]
-[[Category: Structural genomic]]
-[[Category: Carveol dehydrogenase]]
-[[Category: Mycobacterium]]
-[[Category: Nad]]
-[[Category: Non-pathogenic strain]]
-[[Category: Ortholog]]
-[[Category: Oxidoreductase]]
-[[Category: Ssgcid]]
-[[Category: Tuberculosis]]

3pxx

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Crystal structure of carveol dehydrogenase from Mycobacterium avium bound to nicotinamide adenine dinucleotide

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