1g63: Difference between revisions

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[[Image:1g63.gif|left|200px]]
{{Seed}}
[[Image:1g63.png|left|200px]]


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{{STRUCTURE_1g63|  PDB=1g63  |  SCENE=  }}  
{{STRUCTURE_1g63|  PDB=1g63  |  SCENE=  }}  


'''PEPTIDYL-CYSTEINE DECARBOXYLASE EPID'''
===PEPTIDYL-CYSTEINE DECARBOXYLASE EPID===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11101502}}


==About this Structure==
==About this Structure==
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[[Category: Beta protein]]
[[Category: Beta protein]]
[[Category: Rossmann like fold]]
[[Category: Rossmann like fold]]
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