1g63

<StructureSection load='1g63' size='340' side='right' caption='[[1g63]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[1g63]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"albococcus_epidermidis"_winslow_and_winslow_1908 "albococcus epidermidis" winslow and winslow 1908]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G63 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G63 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g5q|1g5q]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EPID ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1282 "Albococcus epidermidis" Winslow and Winslow 1908])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1g63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g63 RCSB], [http://www.ebi.ac.uk/pdbsum/1g63 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g63 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/EPID_STAEP EPID_STAEP]] Catalyzes the removal of two reducing equivalents (oxidative decarboxylation) from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11101502</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1g63" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Albococcus epidermidis winslow and winslow 1908]]

[[Category: Blaesse, M]]

[[Category: Huber, R]]

[[Category: Kupke, T]]

[[Category: Steinbac, S]]

[[Category: Rossmann like fold]]