1g5q
From Proteopedia
(New page: 200px<br /><applet load="1g5q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g5q, resolution 2.57Å" /> '''EPID H67N COMPLEXED ...) |
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| - | [[Image:1g5q.jpg|left|200px]]<br /><applet load="1g5q" size=" | + | [[Image:1g5q.jpg|left|200px]]<br /><applet load="1g5q" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g5q, resolution 2.57Å" /> | caption="1g5q, resolution 2.57Å" /> | ||
'''EPID H67N COMPLEXED WITH SUBSTRATE PEPTIDE DSYTC'''<br /> | '''EPID H67N COMPLEXED WITH SUBSTRATE PEPTIDE DSYTC'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Epidermin from Staphylococcus epidermidis Tu3298 is an antimicrobial | + | 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== | ==About this Structure== | ||
| - | 1G5Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_epidermidis Staphylococcus epidermidis] with FMN and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1G5Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_epidermidis Staphylococcus epidermidis] with <scene name='pdbligand=FMN:'>FMN</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G5Q OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rossman like fold]] | [[Category: rossman like fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:26 2008'' |
Revision as of 10:46, 21 February 2008
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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 with and as ligands. 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 Feb 21 12:46:26 2008
