Annotation

Description

Aminoglycosides comprise a large, structurally diverse family of water-soluble polycationic antibiotics, such as gentamicin and kanamycin (Azucena and Mobashery, 2001). mechanisms. Aminoglycoside N-acetyltransferases (AACs) serve as one component of the bacterical antibiotic resistance mechanisms against aminoglycosides. By acetylating amino groups in an acetyl-CoA-dependent manner, these enzymes are capable of abolishing the activity of these antibiotics (Llano-Sotelo, 2002). This structure is that of the apo-form of the putative aminoglycoside N-acetyltransferase BA2930 from Bacillus anthracis. Analysis of the structure indicates that it possesses a characteristic fold identified for only one other N-acetyltransferase, that of the Antibiotic_NAT family from Bacillus subtilis (PDB code 2NYG). Analysis of the binding mode of the ligands for the enzyme may significantly contribute to existing knowledge of the mechanisms of anthrax drug resistance.  

Functional assignment

aminoglycoside N-acetyltransferase 

Structure information

Unit cell parameters

Space Group

P 21 21 21  

Unit Cell

a=36.31Å, b=108.05Å, c=132.81Å
α=90.00, β=90.00, γ=90.00 

Solvent content

43.22  

Matthews coefficient

2.17  

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

50.00-2.00Å (2.05-2.00Å)  

R_all(%)

17.5 

R_work(%)

17.3 (16.9) 

R_free(%)

22.6 (23.8) 

Num. observed reflections

36210 (2560) 

Num. R_free reflections

1810 (112) 

Completeness(%)

99.7 (97.5) 

Model parameters

Num Atoms

3976  

Num Waters

293  

Num Hetatoms

405  

Model mean isotropic B factor

25.853Ų  

RMSD bond length

0.017Å  

RMSD bond angle

1.666°  

Filename uploaded

BA2930_native_refmac11.pdb (uploaded on Oct 27, 2008 12:52 PM)  

Inserted

Oct 27, 2008