1b87
From Proteopedia
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|PDB= 1b87 |SIZE=350|CAPTION= <scene name='initialview01'>1b87</scene>, resolution 2.70Å | |PDB= 1b87 |SIZE=350|CAPTION= <scene name='initialview01'>1b87</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACO:ACETYL COENZYME *A'>ACO</scene> | + | |LIGAND= <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b87 OCA], [http://www.ebi.ac.uk/pdbsum/1b87 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b87 RCSB]</span> | ||
}} | }} | ||
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[[Category: Berghuis, A M.]] | [[Category: Berghuis, A M.]] | ||
[[Category: Wybenga-Groot, L E.]] | [[Category: Wybenga-Groot, L E.]] | ||
| - | [[Category: ACO]] | ||
[[Category: acetyl coenzyme some]] | [[Category: acetyl coenzyme some]] | ||
[[Category: aminoglycoside 6'-n-acetyltransferase]] | [[Category: aminoglycoside 6'-n-acetyltransferase]] | ||
[[Category: antibiotic resistance]] | [[Category: antibiotic resistance]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:55:34 2008'' |
Revision as of 15:55, 30 March 2008
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| , resolution 2.70Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF AN AMINOGLYCOSIDE 6'-N-ACETYLTRANSFERASE
Overview
BACKGROUND: The predominant mechanism of antibiotic resistance employed by pathogenic bacteria against the clinically used aminoglycosides is chemical modification of the drug. The detoxification reactions are catalyzed by enzymes that promote either the phosphorylation, adenylation or acetylation of aminoglycosides. Structural studies of these aminoglycoside-modifying enzymes may assist in the development of therapeutic agents that could circumvent antibiotic resistance. In addition, such studies may shed light on the development of antibiotic resistance and the evolution of different enzyme classes. RESULTS: The crystal structure of the aminoglycoside-modifying enzyme aminoglycoside 6'-N-acetyltransferase type li (AAC(6')-li) in complex with the cofactor acetyl coenzyme A has been determined at 2.7 A resolution. The structure establishes that this acetyltransferase belongs to the GCN5-related N-acetyltransferase superfamily, which includes such enzymes as the histone acetyltransferases GCN5 and Hat1. CONCLUSIONS: Comparison of the AAC(6')-li structure with the crystal structures of two other members of this superfamily, Serratia marcescens aminoglycoside 3-N-acetyltransferase and yeast histone acetyltransferase Hat1, reveals that of the 84 residues that are structurally similar, only three are conserved and none can be implicated as catalytic residues. Despite the negligible sequence identity, functional studies show that AAC(6')-li possesses protein acetylation activity. Thus, AAC(6')-li is both a structural and functional homolog of the GCN5-related histone acetyltransferases.
About this Structure
1B87 is a Single protein structure of sequence from Enterococcus faecium. Full crystallographic information is available from OCA.
Reference
Crystal structure of an aminoglycoside 6'-N-acetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold., Wybenga-Groot LE, Draker K, Wright GD, Berghuis AM, Structure. 1999 May;7(5):497-507. PMID:10378269
Page seeded by OCA on Sun Mar 30 18:55:34 2008
