1m4d
From Proteopedia
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|PDB= 1m4d |SIZE=350|CAPTION= <scene name='initialview01'>1m4d</scene>, resolution 1.8Å | |PDB= 1m4d |SIZE=350|CAPTION= <scene name='initialview01'>1m4d</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=PAP:3'-PHOSPHATE-ADENOSINE-5'-DIPHOSPHATE'>PAP</scene>, <scene name='pdbligand=TOY:TOBRAMYCIN'>TOY</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1m44|1M44]], [[1m4g|1M4G]], [[1m4i|1M4I]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4d OCA], [http://www.ebi.ac.uk/pdbsum/1m4d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m4d RCSB]</span> | ||
}} | }} | ||
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[[Category: Roderick, S L.]] | [[Category: Roderick, S L.]] | ||
[[Category: Vetting, M W.]] | [[Category: Vetting, M W.]] | ||
| - | [[Category: COA]] | ||
| - | [[Category: PAP]] | ||
| - | [[Category: TOY]] | ||
[[Category: coa binding motif]] | [[Category: coa binding motif]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:11:03 2008'' |
Revision as of 19:11, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1M44, 1M4G, 1M4I
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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