Center for Structural Genomics of Infectious Diseases

To see full content of that page you need the activeISee plugin.
Get the latest version from here.

Structure of IDP00624

CSGID target: IDP00624
PDB Id: 3QFH (NCBI MMDB)
Authors: G.Minasov,A.Halavaty,L.Shuvalova,I.Dubrovska,J.Winsor,F.Bagnoli,F.Falugi,M.Bottomley,G.Grandi,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)
Responsible person: George Minasov
Responsible lab: Northwestern University
Deposition Date: Jan 21, 2011
Release Date: Feb 02, 2011

Description: Epidermin is a 21-amino acid lantibiotic that has antimicrobial activity toward gram-positive bacteria. It is produced and processed through a series of proteins to form the mature epidermin. EpiP is one of the proteins in the cascade to produce this mature lantibiotic. EpiP is intracellularly produced and is then transported across the cell membrane where it is attached to the surface of the cell. It is puzzling as to why Staphylococcus aureus has this protein since it does not produce epidermin and is lacking several of the genes for its production. The EpiP protein from Staphylococcus aureus shows similarity to subtilisin-like serine proteases, and has conserved residues (Asp140, His 187, and Ser393) corresponding to the catalytic triad for serine proteases. In our wild-type structure the polypeptide chain has been cleaved somewhere between residues 95 and 100, indicating that the cleavage may have been autocatalytic. To determine if the protein is acting like a subtilisin-like serine protease, we mutated the hypothesized catalytic serine residue to alanine. The crystal structure of this mutant protein shows that the polypeptide chain is not cleaved and is not interacting with the active site.
Functional assignment: subtilisin-like serine proteases

Ligand code	Name	Ligand type
NA		crystallization
GOL	glycerol	crystallization
EDO	ethylene diol	crystallization
175	3,5-dihydro-5-methylidene-4h-imidazol-4-on