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2jgp
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of the bidomain PCP-C from modules 5 and 6 of the | + | 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== | ==About this Structure== | ||
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[[Category: Brevibacillus brevis]] | [[Category: Brevibacillus brevis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Essen, L | + | [[Category: Essen, L O.]] |
| - | [[Category: Knappe, T | + | [[Category: Knappe, T A.]] |
| - | [[Category: Marahiel, M | + | [[Category: Marahiel, M A.]] |
| - | [[Category: Samel, S | + | [[Category: Samel, S A.]] |
[[Category: Schoenafinger, G.]] | [[Category: Schoenafinger, G.]] | ||
[[Category: DIO]] | [[Category: DIO]] | ||
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[[Category: tyrocidine]] | [[Category: tyrocidine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:03:09 2008'' |
Revision as of 16:03, 21 February 2008
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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 with , and as ligands. Known structural/functional Sites: , , , and . 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 Thu Feb 21 18:03:09 2008
Categories: Brevibacillus brevis | Single protein | Essen, L O. | Knappe, T A. | Marahiel, M A. | Samel, S A. | Schoenafinger, G. | DIO | NA | SO4 | Antibiotic biosynthesis | Antibiotics | Condensation domain | Ligase | Multifunctional enzyme | Nonribosomal peptide synthetase | Peptide bond formation | Peptidyl carrier domain | Phosphopantetheine | Tyrocidine
