Annotation

Description

Microcins are small antibiotic peptides secreted by enterobacteria. They play a critical role in mediating competition between closely related bacterial strains. The 3-dimentional structures and antibacterial mechanisms of these peptide toxins are diverse. The production, maturation, and export requires several enzymes and proteins. The MccF microcin immunity protein from Bacillus anthracis Ames strain(BaMccF) was revealed to be a homodimer and shares fold similarity with LD-carboxypeptidases(LdCa). Fold and sequence analysis revealed that MccF may act as a serine peptidase using a catalytic triad composed of Ser-His-Glu. Superimposition of BaMccf over LdCa revealed similar fold. The main difference between both structures is presence of a 27 residues insertion that forms long loop involved in binding of AMP. Mutation studies revealed possible role of the certain residues in a substrate binding.  

Functional assignment

MccF-like protein 

Structure information

Unit cell parameters

Space Group

P 43  

Unit Cell

a=118.23Å, b=118.23Å, c=54.84Å
α=90.00, β=90.00, γ=90.00 

Solvent content

 

Matthews coefficient

 

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

40.00-2.04Å (2.10-2.04Å)  

R_all(%)

16.9 

R_work(%)

16.7 (24.5) 

R_free(%)

21.0 (30.1) 

Num. observed reflections

47213 (2801) 

Num. R_free reflections

2407 (136) 

Completeness(%)

97.6 (81.4) 

Model parameters

Num Atoms

5615  

Num Waters

260  

Num Hetatoms

0  

Model mean isotropic B factor

39.500Ų  

RMSD bond length

0.016Å  

RMSD bond angle

1.882°  

Filename uploaded

F177S-amp_refine_12_FINAL.pdb (uploaded on Sep 28, 2011 4:22 PM)  

Inserted

Sep 28, 2011