1g63
From Proteopedia
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PEPTIDYL-CYSTEINE DECARBOXYLASE EPID
Overview
Epidermin from Staphylococcus epidermidis Tu3298 is an antimicrobial, peptide of the lantibiotic family that contains, amongst other unusual, amino acids, S:-[(Z:)- 2-aminovinyl]-D-cysteine. This residue is, introduced by post-translational modification of the ribosomally, synthesized precursor EpiA. Modification starts with the oxidative, decarboxylation of its C-terminal cysteine by the flavoprotein EpiD, generating a reactive (Z:)-enethiol intermediate. We have determined the, crystal structures of EpiD and EpiD H67N in complex with the substrate, pentapeptide DSYTC at 2.5 A resolution. Rossmann-type monomers build up a, dodecamer of 23 point symmetry with trimers disposed at the vertices of a, tetrahedron. Oligomer formation is essential for binding of flavin, mononucleotide and substrate, which is buried by an otherwise disordered, substrate recognition clamp. A pocket for the tyrosine residue of the, substrate peptide is formed by an induced fit mechanism. The substrate, contacts flavin mononucleotide only via Cys-Sgamma, suggesting its, oxidation as the initial step. A thioaldehyde intermediate could undergo, spontaneous decarboxylation. The unusual substrate recognition mode and, the type of chemical reaction performed provide insight into a novel, family of flavoproteins.
About this Structure
1G63 is a Single protein structure of sequence from Staphylococcus epidermidis with FMN as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate., Blaesse M, Kupke T, Huber R, Steinbacher S, EMBO J. 2000 Dec 1;19(23):6299-310. PMID:11101502
Page seeded by OCA on Tue Nov 20 15:44:22 2007
