1g63
From Proteopedia
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| - | [[Image:1g63.gif|left|200px]] | + | [[Image:1g63.gif|left|200px]] |
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| - | '''PEPTIDYL-CYSTEINE DECARBOXYLASE EPID''' | + | {{Structure |
| + | |PDB= 1g63 |SIZE=350|CAPTION= <scene name='initialview01'>1g63</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FMN:FLAVIN MONONUCLEOTIDE'>FMN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= EPID ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1282 Staphylococcus epidermidis]) | ||
| + | }} | ||
| + | |||
| + | '''PEPTIDYL-CYSTEINE DECARBOXYLASE EPID''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G63 is a [ | + | 1G63 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_epidermidis Staphylococcus epidermidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G63 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11101502 11101502] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus epidermidis]] | [[Category: Staphylococcus epidermidis]] | ||
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[[Category: rossmann like fold]] | [[Category: rossmann like fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:18:43 2008'' |
Revision as of 09:18, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Ligands: | |||||||
| Gene: | EPID (Staphylococcus epidermidis) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 11:18:43 2008
