View source for 4bgf


==The 3D-structure of arylamine-N-acetyltransferase from M. tuberculosis==
<StructureSection load='4bgf' size='340' side='right'caption='[[4bgf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bgf]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BGF 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]] 2.097&#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=4bgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bgf OCA], [https://pdbe.org/4bgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bgf RCSB], [https://www.ebi.ac.uk/pdbsum/4bgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bgf ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Arylamine N-acetyltransferase from Mycobacterium tuberculosis (TBNAT) plays an important role in the intracellular survival of the microorganism inside macrophages. Medicinal chemistry efforts to optimize inhibitors of the TBNAT enzyme have been hampered by the lack of a three-dimensional structure of the enzyme. In this paper, the first structure of TBNAT, determined using a lone crystal produced using cross-seeding with the homologous protein from M. marinum, is reported. Despite the similarity between the two enzymes (74% sequence identity), they show distinct physical and biochemical characteristics. The structure elegantly reveals the characteristic features of the protein surface as well as details of the active site of TBNAT relevant to drug-discovery efforts. The crystallographic analysis of the diffraction data presented many challenges, since the crystal was twinned and the habit possessed pseudo-translational symmetry.

Structure of arylamine N-acetyltransferase from Mycobacterium tuberculosis determined by cross-seeding with the homologous protein from M. marinum: triumph over adversity.,Abuhammad A, Lowe ED, McDonough MA, Shaw Stewart PD, Kolek SA, Sim E, Garman EF Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1433-46. doi:, 10.1107/S0907444913015126. Epub 2013 Jul 17. PMID:23897467<ref>PMID:23897467</ref>

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

==See Also==
*[[Arylamine N-acetyltransferase 3D structures|Arylamine N-acetyltransferase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Abuhammad A]]
[[Category: Garman EF]]
[[Category: Kolek SA]]
[[Category: Lowe ED]]
[[Category: McDonough MA]]
[[Category: Shaw Stewart PD]]
[[Category: Sim E]]