3ltw

<StructureSection load='3ltw' size='340' side='right' caption='[[3ltw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[3ltw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycmm Mycmm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LTW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LTW FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=HLZ:1-HYDRAZINOPHTHALAZINE'>HLZ</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vfb|2vfb]], [[2vfc|2vfc]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nat, MMAR_5055 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216594 MYCMM])</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=3ltw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ltw OCA], [http://pdbe.org/3ltw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ltw RCSB], [http://www.ebi.ac.uk/pdbsum/3ltw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ltw ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Treatment of latent tuberculosis infection remains an important goal of global TB eradication. To this end, targets that are essential for intracellular survival of Mycobacterium tuberculosis are particularly attractive. Arylamine N-acetyltransferase (NAT) represents such a target as it is, along with the enzymes encoded by the associated gene cluster, essential for mycobacterial survival inside macrophages and involved in cholesterol degradation. Cholesterol is likely to be the fuel for M. tuberculosis inside macrophages. Deleting the nat gene and inhibiting the NAT enzyme prevents survival of the microorganism in macrophages and induces cell wall alterations, rendering the mycobacterium sensitive to antibiotics to which it is normally resistant. To date, NAT from M. marinum (MMNAT) is considered the best available model for NAT from M. tuberculosis (TBNAT). The enzyme catalyses the acetylation and propionylation of arylamines and hydrazines. Hydralazine is a good acetyl and propionyl acceptor for both MMNAT and TBNAT. The MMNAT structure has been solved to 2.1 A resolution following crystallisation in the presence of hydralazine and is compared to available NAT structures. From the mode of ligand binding, features of the binding pocket can be identified, which point to a novel mechanism for the acetylation reaction that results in a 3-methyltriazolo[3,4-a]phthalazine ring compound as product.

Probing the architecture of the Mycobacterium marinum arylamine N-acetyltransferase active site.,Abuhammad AM, Lowe ED, Fullam E, Noble M, Garman EF, Sim E Protein Cell. 2010 Apr;1(4):384-92. Epub 2010 May 8. PMID:21203950<ref>PMID:21203950</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 3ltw" style="background-color:#fffaf0;"></div>

*[[Arylamine N-acetyltransferase|Arylamine N-acetyltransferase]]

[[Category: Arylamine N-acetyltransferase]]

[[Category: Mycmm]]

[[Category: Abuhammad, A M]]

[[Category: Fullam, E]]

[[Category: Garman, E F]]

[[Category: Lowe, E D]]

[[Category: Noble, M]]

[[Category: Sim, E]]

[[Category: Transferase]]