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| | ==Crystal structure of a putative carveol dehydrogenase from Mycobacterium paratuberculosis bound to nicotinamide adenine dinucleotide== | | ==Crystal structure of a putative carveol dehydrogenase from Mycobacterium paratuberculosis bound to nicotinamide adenine dinucleotide== |
| - | <StructureSection load='3pgx' size='340' side='right' caption='[[3pgx]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='3pgx' size='340' side='right'caption='[[3pgx]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pgx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_paratuberculosis"_(bergey_et_al._1923)_krasil'nikov_1941 "bacillus paratuberculosis" (bergey et al. 1923) krasil'nikov 1941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PGX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PGX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3pgx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_avium_subsp._paratuberculosis Mycobacterium avium subsp. paratuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PGX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.85Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3oec|3oec]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAP_4146 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1770 "Bacillus paratuberculosis" (Bergey et al. 1923) Krasil'nikov 1941])</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=3pgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pgx OCA], [https://pdbe.org/3pgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pgx RCSB], [https://www.ebi.ac.uk/pdbsum/3pgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pgx ProSAT]</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=3pgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pgx OCA], [http://pdbe.org/3pgx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pgx RCSB], [http://www.ebi.ac.uk/pdbsum/3pgx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pgx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Y4146_MYCPA Y4146_MYCPA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3pgx" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3pgx" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[User:Wayne Decatur/UNH BCHEM833 Structural Analysis Workshop Session Fall 2012|User:Wayne Decatur/UNH BCHEM833 Structural Analysis Workshop Session Fall 2012]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Structural genomic]] | + | [[Category: Large Structures]] |
| - | [[Category: Carveol dehydrogenase]] | + | [[Category: Mycobacterium avium subsp. paratuberculosis]] |
| - | [[Category: Nad]]
| + | |
| - | [[Category: Nicotinamide adenine dinucleotide]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Putative uncharacterized protein]]
| + | |
| - | [[Category: Short chain dehydrogenase/reductase superfamily]]
| + | |
| - | [[Category: Ssgcid]]
| + | |
| Structural highlights
Function
Y4146_MYCPA
Publication Abstract from PubMed
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors. Sci Rep. 2017 Jan 25;7:41074. doi: 10.1038/srep41074. PMID:28120876 doi:http://dx.doi.org/10.1038/srep41074
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