1m44
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(New page: 200px<br /><applet load="1m44" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m44, resolution 1.6Å" /> '''Aminoglycoside 2'-N-a...)
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Revision as of 19:00, 20 November 2007
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Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-APO Structure
Overview
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.
About this Structure
1M44 is a Single protein structure of sequence from Mycobacterium tuberculosis with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
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
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