1jmk

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[[Image:1jmk.jpg|left|200px]]
[[Image:1jmk.jpg|left|200px]]
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{{Structure
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|PDB= 1jmk |SIZE=350|CAPTION= <scene name='initialview01'>1jmk</scene>, resolution 1.71&Aring;
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The line below this paragraph, containing "STRUCTURE_1jmk", creates the "Structure Box" on the page.
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|GENE= SrfA-C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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{{STRUCTURE_1jmk| PDB=1jmk | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jmk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jmk OCA], [http://www.ebi.ac.uk/pdbsum/1jmk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jmk RCSB]</span>
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'''Structural Basis for the Cyclization of the Lipopeptide Antibiotic Surfactin by the Thioesterase Domain SrfTE'''
'''Structural Basis for the Cyclization of the Lipopeptide Antibiotic Surfactin by the Thioesterase Domain SrfTE'''
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[[Category: Walsh, C T.]]
[[Category: Walsh, C T.]]
[[Category: Weber, T.]]
[[Category: Weber, T.]]
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[[Category: alpha-beta hydrolase]]
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[[Category: Alpha-beta hydrolase]]
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[[Category: cyclic peptide]]
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[[Category: Cyclic peptide]]
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[[Category: non-ribosomal peptide synthesis]]
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[[Category: Non-ribosomal peptide synthesis]]
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[[Category: thioesterase]]
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[[Category: Thioesterase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:24:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:35:51 2008''
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Revision as of 18:24, 2 May 2008

Template:STRUCTURE 1jmk

Structural Basis for the Cyclization of the Lipopeptide Antibiotic Surfactin by the Thioesterase Domain SrfTE


Overview

Many biologically active natural peptides are synthesized by nonribosomal peptide synthetases (NRPS). Product release is accomplished by dedicated thioesterase (TE) domains, some of which catalyze an intramolecular cyclization to form macrolactone or macrolactam cyclic peptides. The excised 28 kDa SrfTE domain, a member of the alpha/beta hydrolase enzyme family, exhibits a distinctive bowl-shaped hydrophobic cavity that hosts the acylpeptide substrate and tolerates its folding to form a cyclic structure. A substrate analog confirms the substrate binding site and suggests a mechanism for substrate acylation/deacylation. Docking of the peptidyl carrier protein domain immediately preceding SrfTE positions the 4'-phosphopantheinyl prosthetic group that transfers the nascent acyl-peptide chain to SrfTE. The structure provides a basis for understanding the mechanism of acyl-PCP substrate recognition and for the cyclization reaction that results in release of the macrolactone cyclic heptapeptide.

About this Structure

1JMK is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Structural basis for the cyclization of the lipopeptide antibiotic surfactin by the thioesterase domain SrfTE., Bruner SD, Weber T, Kohli RM, Schwarzer D, Marahiel MA, Walsh CT, Stubbs MT, Structure. 2002 Mar;10(3):301-10. PMID:12005429 Page seeded by OCA on Fri May 2 21:24:53 2008

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