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 was revealed to be a homodimer and shares fold similarity with LD-carboxypeptidases. Fold and sequence analysis revealed that MccF may act as a serine peptidase using a catalytic triad composed of Ser-His-Glu. The figure shows a ribbon representation of the MccF structure (PDB code: 3GJZ), with monomers colored in orange and green. The catalytic triad residues are shown as blue sticks.
Information for researchers about this micorcin structure can be found at the CSGID summary, http://www.csgid.org/csgid/cake/deposits/view/1023, or the Protein Data Bank entry 3GJZ, http://www.pdb.org/pdb/explore/explore.do?structureId=3GJZ.
All featured structures from the NIAID Structural Genomics Centers
Last Updated July 27, 2010