View source for 3lnb


==Crystal Structure Analysis of Arylamine N-acetyltransferase C from Bacillus anthracis==
<StructureSection load='3lnb' size='340' side='right'caption='[[3lnb]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3lnb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LNB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LNB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=3lnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lnb OCA], [https://pdbe.org/3lnb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lnb RCSB], [https://www.ebi.ac.uk/pdbsum/3lnb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lnb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A6L7HKL6_BACAN A0A6L7HKL6_BACAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Arylamine N-acetyltransferases (NATs) are xenobiotic-metabolizing enzymes that biotransform arylamine drugs. The Bacillus anthracis (BACAN)NAT1 enzyme affords increased resistance to the antibiotic sulfamethoxazole through its acetylation. We report the structure of (BACAN)NAT1. Unexpectedly, endogenous coenzymeA was present in the active site. The structure suggests that, contrary to the other prokaryotic NATs, (BACAN)NAT1 possesses a 14-residue insertion equivalent to the "mammalian insertion", a structural feature considered unique to mammalian NATs. Moreover, (BACAN)NAT1 structure shows marked differences in the mode of binding and location of coenzymeA when compared to the other NATs. This suggests that the mechanisms of cofactor recognition by NATs is more diverse than expected and supports the cofactor-binding site as being a unique subsite to target in drug design against bacterial NATs.

The Bacillus anthracis arylamine N-acetyltransferase ((BACAN)NAT1) that inactivates sulfamethoxazole, reveals unusual structural features compared with the other NAT isoenzymes.,Pluvinage B, Li de la Sierra-Gallay I, Kubiak X, Xu X, Dairou J, Dupret JM, Rodrigues-Lima F FEBS Lett. 2011 Dec 15;585(24):3947-52. Epub 2011 Nov 2. PMID:22062153<ref>PMID:22062153</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3lnb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Arylamine N-acetyltransferase 3D structures|Arylamine N-acetyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus anthracis]]
[[Category: Large Structures]]
[[Category: Li de la Sierra-Gallay I]]
[[Category: Pluvinage B]]
[[Category: Rodrigues-Lima F]]