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{{STRUCTURE_2jgp| PDB=2jgp | SCENE= }} | |||
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'''STRUCTURE OF THE TYCC5-6 PCP-C BIDOMAIN OF THE TYROCIDINE SYNTHETASE TYCC''' | '''STRUCTURE OF THE TYCC5-6 PCP-C BIDOMAIN OF THE TYROCIDINE SYNTHETASE TYCC''' | ||
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[[Category: Samel, S A.]] | [[Category: Samel, S A.]] | ||
[[Category: Schoenafinger, G.]] | [[Category: Schoenafinger, G.]] | ||
[[Category: | [[Category: Antibiotic biosynthesis]] | ||
[[Category: | [[Category: Antibiotic]] | ||
[[Category: | [[Category: Condensation domain]] | ||
[[Category: | [[Category: Ligase]] | ||
[[Category: | [[Category: Multifunctional enzyme]] | ||
[[Category: | [[Category: Nonribosomal peptide synthetase]] | ||
[[Category: | [[Category: Peptide bond formation]] | ||
[[Category: | [[Category: Peptidyl carrier domain]] | ||
[[Category: | [[Category: Phosphopantetheine]] | ||
[[Category: | [[Category: Tyrocidine]] | ||
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Revision as of 05:53, 4 May 2008
STRUCTURE OF THE TYCC5-6 PCP-C BIDOMAIN OF THE TYROCIDINE SYNTHETASE TYCC
Overview
The crystal structure of the bidomain PCP-C from modules 5 and 6 of the nonribosomal tyrocidine synthetase TycC was determined at 1.8 A resolution. The bidomain structure reveals a V-shaped condensation domain, the canyon-like active site groove of which is associated with the preceding peptidyl carrier protein (PCP) domain at its donor side. The relative arrangement of the PCP and the peptide bond-forming condensation (C) domain places the active sites approximately 50 A apart. Accordingly, this PCP-C structure represents a conformational state prior to peptide transfer from the donor-PCP to the acceptor-PCP domain, implying the existence of additional states of PCP-C domain interaction during catalysis. Additionally, PCP-C exerts a mode of cyclization activity that mimics peptide bond formation catalyzed by C domains. Based on mutational data and pK value analysis of active site residues, it is suggested that nonribosomal peptide bond formation depends on electrostatic interactions rather than on general acid/base catalysis.
About this Structure
2JGP is a Single protein structure of sequence from Brevibacillus brevis. Full crystallographic information is available from OCA.
Reference
Structural and functional insights into a peptide bond-forming bidomain from a nonribosomal peptide synthetase., Samel SA, Schoenafinger G, Knappe TA, Marahiel MA, Essen LO, Structure. 2007 Jul;15(7):781-92. PMID:17637339 Page seeded by OCA on Sun May 4 08:53:16 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Brevibacillus brevis
- Single protein
- Essen, L O.
- Knappe, T A.
- Marahiel, M A.
- Samel, S A.
- Schoenafinger, G.
- Antibiotic biosynthesis
- Antibiotic
- Condensation domain
- Ligase
- Multifunctional enzyme
- Nonribosomal peptide synthetase
- Peptide bond formation
- Peptidyl carrier domain
- Phosphopantetheine
- Tyrocidine