3d9w
From Proteopedia
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| - | + | ==Crystal Structure Analysis of Nocardia farcinica Arylamine N-acetyltransferase== | |
| - | === | + | <StructureSection load='3d9w' size='340' side='right' caption='[[3d9w]], [[Resolution|resolution]] 2.70Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3d9w]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_bovis_farcinicus"_gasperini_1894 "actinomyces bovis farcinicus" gasperini 1894]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D9W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D9W FirstGlance]. <br> | ||
| + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nfa18420 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37329 "Actinomyces bovis farcinicus" Gasperini 1894])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arylamine_N-acetyltransferase Arylamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.5 2.3.1.5] </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=3d9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d9w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3d9w RCSB], [http://www.ebi.ac.uk/pdbsum/3d9w PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d9/3d9w_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Arylamine N-acetyltransferase (NAT) enzymes are found in a broad range of eukaryotes and prokaryotes. There is increasing evidence that NAT enzymes could contribute to antibiotic resistance in pathogenic bacteria such as Mycobacterium tuberculosis. Nocardia farcinica is an opportunistic human pathogen that causes pulmonary infections (nocardiosis) with clinical manifestations that resemble tuberculosis. While the genomic sequence of this prokaryote has been determined, studies of N. farcinica proteins remain almost nonexistent. In particular, N. farcinica proteins putatively involved in antibiotic resistance mechanisms have not been described structurally or functionally. Here, we have characterized a new NAT enzyme (NfNAT) from N. farcinica at the structural and functional level. NfNAT is the first N. farcinica protein for which a 3D structure is reported. We showed that this novel prokaryotic isoform is structurally and functionally related to the mycobacterial NAT enzymes. In particular, NfNAT was found to display high N-acetyltransferase activity towards several known NAT substrates including the antitubercular drug isoniazid. Interestingly, isoniazid is not used for the treatment of nocardiosis and has been shown to be poorly active against several nocardial species. On the contrary, NfNAT was found to be poorly active towards sulfamethoxazole, a sulfonamide drug considered as the treatment of choice for the treatment of nocardiosis. The functional and structural data reported in this study will help to develop our understanding of the role of NAT enzymes in nocardia and mycobacteria and may help in the rational design of NAT antagonists for a range of clinical applications. | ||
| - | + | Functional and structural characterization of the arylamine N-acetyltransferase from the opportunistic pathogen Nocardia farcinica.,Martins M, Pluvinage B, de la Sierra-Gallay IL, Barbault F, Dairou J, Dupret JM, Rodrigues-Lima F J Mol Biol. 2008 Nov 14;383(3):549-60. Epub 2008 Aug 22. PMID:18778714<ref>PMID:18778714</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[Arylamine N-acetyltransferase|Arylamine N-acetyltransferase]] | *[[Arylamine N-acetyltransferase|Arylamine N-acetyltransferase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Actinomyces bovis farcinicus gasperini 1894]] | [[Category: Actinomyces bovis farcinicus gasperini 1894]] | ||
[[Category: Arylamine N-acetyltransferase]] | [[Category: Arylamine N-acetyltransferase]] | ||
| - | [[Category: Dupret, J M | + | [[Category: Dupret, J M]] |
| - | [[Category: Martins, M | + | [[Category: Martins, M]] |
| - | [[Category: Pluvinage, B | + | [[Category: Pluvinage, B]] |
| - | [[Category: Rodrigues-Lima, F | + | [[Category: Rodrigues-Lima, F]] |
| - | [[Category: Sierra-Gallay, I Li de la | + | [[Category: Sierra-Gallay, I Li de la]] |
[[Category: Acyltransferase]] | [[Category: Acyltransferase]] | ||
[[Category: Arylamine n-acetyltransferase]] | [[Category: Arylamine n-acetyltransferase]] | ||
[[Category: Nat]] | [[Category: Nat]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 18:46, 21 December 2014
Crystal Structure Analysis of Nocardia farcinica Arylamine N-acetyltransferase
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