1m44

<StructureSection load='1m44' size='340' side='right' caption='[[1m44]], [[Resolution|resolution]] 1.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[1m44]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M44 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M44 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m4d|1m4d]], [[1m4g|1m4g]], [[1m4i|1m4i]]</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=1m44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m44 OCA], [http://pdbe.org/1m44 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m44 RCSB], [http://www.ebi.ac.uk/pdbsum/1m44 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m44 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/AAC2_MYCTU AAC2_MYCTU]] Catalyzes the coenzyme A-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides. It confers resistance to aminoglycosides.

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== Publication Abstract from PubMed ==

AAC(2')-Ic catalyzes the coenzyme A (CoA)-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides. The crystal structure of the AAC(2')-Ic from Mycobacterium tuberculosis has been determined in the apo enzyme form and in ternary complexes with CoA and either tobramycin, kanamycin A or ribostamycin, representing the first structures of an aminoglycoside acetyltransferase bound to a drug. The overall fold of AAC(2')-Ic places it in the GCN5-related N-acetyltransferase (GNAT) superfamily. Although the physiological function of AAC(2')-Ic is uncertain, a structural analysis of these high-affinity aminoglycoside complexes suggests that the enzyme may acetylate a key biosynthetic intermediate of mycothiol, the major reducing agent in mycobacteria, and participate in the regulation of cellular redox potential.

Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates.,Vetting MW, Hegde SS, Javid-Majd F, Blanchard JS, Roderick SL Nat Struct Biol. 2002 Sep;9(9):653-8. PMID:12161746<ref>PMID:12161746</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 1m44" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Myctu]]

[[Category: Blanchard, J S]]

[[Category: Hegde, S S]]

[[Category: Javid-Majd, F]]

[[Category: Roderick, S L]]

[[Category: Vetting, M W]]

[[Category: Transferase]]