4guz

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==Structure of the arylamine N-acetyltransferase from Mycobacterium abscessus==
==Structure of the arylamine N-acetyltransferase from Mycobacterium abscessus==
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<StructureSection load='4guz' size='340' side='right' caption='[[4guz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='4guz' size='340' side='right'caption='[[4guz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4guz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Myca9 Myca9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GUZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4guz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacteroides_abscessus_ATCC_19977 Mycobacteroides abscessus ATCC 19977]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GUZ FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAB_0013c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=561007 MYCA9])</td></tr>
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</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=4guz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4guz OCA], [https://pdbe.org/4guz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4guz RCSB], [https://www.ebi.ac.uk/pdbsum/4guz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4guz ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-hydroxyarylamine_O-acetyltransferase N-hydroxyarylamine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.118 2.3.1.118] </span></td></tr>
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<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=4guz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4guz OCA], [http://pdbe.org/4guz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4guz RCSB], [http://www.ebi.ac.uk/pdbsum/4guz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4guz ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/B1ME52_MYCA9 B1ME52_MYCA9]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mycobacterium abscessus is the most pathogenic rapid-growing mycobacterium and is one of the most resistant organisms to chemotherapeutic agents. However, structural and functional studies of M. abscessus proteins that could modify/inactivate antibiotics remain nonexistent. Here, the structural and functional characterization of an arylamine N-acetyltransferase (NAT) from M. abscessus [(MYCAB)NAT1] are reported. This novel prokaryotic NAT displays significant N-acetyltransferase activity towards aromatic substrates, including antibiotics such as isoniazid and p-aminosalicylate. The enzyme is endogenously expressed and functional in both the rough and smooth M. abscessus morphotypes. The crystal structure of (MYCAB)NAT1 at 1.8 A resolution reveals that it is more closely related to Nocardia farcinica NAT than to mycobacterial isoforms. In particular, structural and physicochemical differences from other mycobacterial NATs were found in the active site. Peculiarities of (MYCAB)NAT1 were further supported by kinetic and docking studies showing that the enzyme was poorly inhibited by the piperidinol inhibitor of mycobacterial NATs. This study describes the first structure of an antibiotic-modifying enzyme from M. abscessus and provides bases to better understand the substrate/inhibitor-binding specificities among mycobacterial NATs and to identify/optimize specific inhibitors. These data should also contribute to the understanding of the mechanisms that are responsible for the pathogenicity and extensive chemotherapeutic resistance of M. abscessus.
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Structural and functional characterization of an arylamine N-acetyltransferase from the pathogen Mycobacterium abscessus: differences from other mycobacterial isoforms and implications for selective inhibition.,Cocaign A, Kubiak X, Xu X, Garnier G, Li de la Sierra-Gallay I, Chi-Bui L, Dairou J, Busi F, Abuhammad A, Haouz A, Dupret JM, Herrmann JL, Rodrigues-Lima F Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):3066-79. doi:, 10.1107/S1399004714021282. Epub 2014 Oct 29. PMID:25372695<ref>PMID:25372695</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 4guz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Myca9]]
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[[Category: Large Structures]]
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[[Category: N-hydroxyarylamine O-acetyltransferase]]
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[[Category: Mycobacteroides abscessus ATCC 19977]]
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[[Category: Haouz, A]]
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[[Category: Haouz A]]
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[[Category: Kubiak, X]]
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[[Category: Kubiak X]]
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[[Category: Rodrigues-Lima, F]]
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[[Category: Li de la Sierra-Gallay I]]
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[[Category: Sierra-Gallay, I Li de la]]
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[[Category: Rodrigues-Lima F]]
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[[Category: Weber, P]]
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[[Category: Weber P]]
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[[Category: Acetyl coenzymea]]
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[[Category: Acetyltransf_2 transferase]]
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[[Category: Acetyltransferase]]
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[[Category: Cytosol]]
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[[Category: Transferase]]
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Revision as of 07:18, 26 October 2022

Structure of the arylamine N-acetyltransferase from Mycobacterium abscessus

PDB ID 4guz

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