1g5q
From Proteopedia
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|PDB= 1g5q |SIZE=350|CAPTION= <scene name='initialview01'>1g5q</scene>, resolution 2.57Å | |PDB= 1g5q |SIZE=350|CAPTION= <scene name='initialview01'>1g5q</scene>, resolution 2.57Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> | + | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= EPID ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1282 Staphylococcus epidermidis]) | |GENE= EPID ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1282 Staphylococcus epidermidis]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1g63|1G63]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5q OCA], [http://www.ebi.ac.uk/pdbsum/1g5q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g5q RCSB]</span> | ||
}} | }} | ||
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[[Category: Kupke, T.]] | [[Category: Kupke, T.]] | ||
[[Category: Steinbacher, S.]] | [[Category: Steinbacher, S.]] | ||
- | [[Category: FMN]] | ||
- | [[Category: TRS]] | ||
[[Category: alpha]] | [[Category: alpha]] | ||
[[Category: beta protein]] | [[Category: beta protein]] | ||
[[Category: rossman like fold]] | [[Category: rossman like fold]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:37:08 2008'' |
Revision as of 17:37, 30 March 2008
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, resolution 2.57Å | |||||||
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Ligands: | , | ||||||
Gene: | EPID (Staphylococcus epidermidis) | ||||||
Related: | 1G63
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
EPID H67N COMPLEXED WITH SUBSTRATE PEPTIDE DSYTC
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
1G5Q is a Protein complex structure of sequences 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
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