1M4G

Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Ribostamycin

Summary for 1M4G

• Entry DOI: 10.2210/pdb1m4g/pdb
• Related: 1M44 1M4D 1M4I
• Descriptor: Aminoglycoside 2'-N-acetyltransferase, COENZYME A, RIBOSTAMYCIN, ... (5 entities in total)
• Functional Keywords: coa binding motif, transferase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 43585.77

Authors

Vetting, M.W.,Hegde, S.S.,Javid-Majd, F.,Blanchard, J.S.,Roderick, S.L. (deposition date: 2002-07-02, release date: 2002-08-28, Last modification date: 2024-02-14)

Primary citation

Vetting, M.W.,Hegde, S.S.,Javid-Majd, F.,Blanchard, J.S.,Roderick, S.L.
Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates.
Nat.Struct.Biol., 9:653-658, 2002

PubMed Abstract: 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.

PubMed: 12161746
DOI: 10.1038/nsb830

Experimental method

X-RAY DIFFRACTION (1.8 Å)