This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1m4d
From Proteopedia
|
Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Tobramycin
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
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.
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
Page seeded by OCA on Tue Nov 20 21:08:13 2007
