1jmk
From Proteopedia
(New page: 200px<br /><applet load="1jmk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jmk, resolution 1.71Å" /> '''Structural Basis for...) |
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| - | [[Image:1jmk.jpg|left|200px]]<br /><applet load="1jmk" size=" | + | [[Image:1jmk.jpg|left|200px]]<br /><applet load="1jmk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jmk, resolution 1.71Å" /> | caption="1jmk, resolution 1.71Å" /> | ||
'''Structural Basis for the Cyclization of the Lipopeptide Antibiotic Surfactin by the Thioesterase Domain SrfTE'''<br /> | '''Structural Basis for the Cyclization of the Lipopeptide Antibiotic Surfactin by the Thioesterase Domain SrfTE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Many biologically active natural peptides are synthesized by nonribosomal | + | 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== | ==About this Structure== | ||
| - | 1JMK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1JMK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bruner, S | + | [[Category: Bruner, S D.]] |
| - | [[Category: Kohli, R | + | [[Category: Kohli, R M.]] |
| - | [[Category: Marahiel, M | + | [[Category: Marahiel, M A.]] |
[[Category: Schwarzer, D.]] | [[Category: Schwarzer, D.]] | ||
| - | [[Category: Stubbs, M | + | [[Category: Stubbs, M T.]] |
| - | [[Category: Walsh, C | + | [[Category: Walsh, C T.]] |
[[Category: Weber, T.]] | [[Category: Weber, T.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: thioesterase]] | [[Category: thioesterase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:17 2008'' |
Revision as of 11:24, 21 February 2008
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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 with as ligand. 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 Thu Feb 21 13:24:17 2008
