1m4d
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Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Tobramycin
OverviewOverview
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 StructureAbout this Structure
1M4D is a Single protein structure of sequence from Mycobacterium tuberculosis with TOY, COA and PAP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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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