1g63: Difference between revisions
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|PDB= 1g63 |SIZE=350|CAPTION= <scene name='initialview01'>1g63</scene>, resolution 2.50Å | |PDB= 1g63 |SIZE=350|CAPTION= <scene name='initialview01'>1g63</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=FMN:FLAVIN MONONUCLEOTIDE'>FMN</scene> | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=[[1g5q|1G5Q]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g63 OCA], [http://www.ebi.ac.uk/pdbsum/1g63 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g63 RCSB]</span> | |||
}} | }} | ||
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[[Category: Kupke, T.]] | [[Category: Kupke, T.]] | ||
[[Category: Steinbac, S.]] | [[Category: Steinbac, S.]] | ||
[[Category: alpha]] | [[Category: alpha]] | ||
[[Category: beta protein]] | [[Category: beta protein]] | ||
[[Category: rossmann like fold]] | [[Category: rossmann 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 20:37:23 2008'' | ||
Revision as of 20:37, 30 March 2008
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| , resolution 2.50Å | |||||||
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| Ligands: | |||||||
| Gene: | EPID (Staphylococcus epidermidis) | ||||||
| Related: | 1G5Q
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PEPTIDYL-CYSTEINE DECARBOXYLASE EPID
OverviewOverview
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 StructureAbout this Structure
1G63 is a Single protein structure of sequence from Staphylococcus epidermidis. Full crystallographic information is available from OCA.
ReferenceReference
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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