View source for 4nv8


==Crystal Structure of Mesorhizobium Loti Arylamine N-acetyltransferase F42W Mutant==
<StructureSection load='4nv8' size='340' side='right'caption='[[4nv8]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4nv8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesorhizobium_japonicum_MAFF_303099 Mesorhizobium japonicum MAFF 303099]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NV8 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]] 1.84&#8491;</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=4nv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nv8 OCA], [https://pdbe.org/4nv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nv8 RCSB], [https://www.ebi.ac.uk/pdbsum/4nv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nv8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q98D42_RHILO Q98D42_RHILO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Arylamine N-acetyltransferases (NATs) are xenobiotic metabolizing enzymes that catalyze the acetyl-CoA-dependent acetylation of arylamines. To better understand the mode of binding of the cofactor by this family of enzymes, the structure of Mesorhizobium loti NAT1 [(RHILO)NAT1] was determined in complex with CoA. The F42W mutant of (RHILO)NAT1 was used as it is well expressed in Escherichia coli and displays enzymatic properties similar to those of the wild type. The apo and holo structures of (RHILO)NAT1 F42W were solved at 1.8 and 2 A resolution, respectively. As observed in the Mycobacterium marinum NAT1-CoA complex, in (RHILO)NAT1 CoA binding induces slight structural rearrangements that are mostly confined to certain residues of its `P-loop'. Importantly, it was found that the mode of binding of CoA is highly similar to that of M. marinum NAT1 but different from the modes reported for Bacillus anthracis NAT1 and Homo sapiens NAT2. Therefore, in contrast to previous data, this study shows that different orthologous NATs can bind their cofactors in a similar way, suggesting that the mode of binding CoA in this family of enzymes is less diverse than previously thought. Moreover, it supports the notion that the presence of the `mammalian/eukaryotic insertion loop' in certain NAT enzymes impacts the mode of binding CoA by imposing structural constraints.

Insight into cofactor recognition in arylamine N-acetyltransferase enzymes: structure of Mesorhizobium loti arylamine N-acetyltransferase in complex with coenzyme A.,Xu X, Li de la Sierra-Gallay I, Kubiak X, Duval R, Chaffotte AF, Dupret JM, Haouz A, Rodrigues-Lima F Acta Crystallogr D Biol Crystallogr. 2015 Feb;71(Pt 2):266-73. doi:, 10.1107/S139900471402522X. Epub 2015 Jan 23. PMID:25664736<ref>PMID:25664736</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4nv8" style="background-color:#fffaf0;"></div>

==See Also==
*[[Arylamine N-acetyltransferase 3D structures|Arylamine N-acetyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mesorhizobium japonicum MAFF 303099]]
[[Category: Dupret J-M]]
[[Category: Haouz A]]
[[Category: Kubiak X]]
[[Category: Li de la sierra-gallay I]]
[[Category: Rodrigues-lima F]]
[[Category: Weber P]]
[[Category: Xu XM]]