2jgp
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2jgp.gif|left|200px]] | [[Image:2jgp.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2jgp", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_2jgp| PDB=2jgp | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''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''' | ||
| Line 30: | Line 27: | ||
[[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]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:53:16 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
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
Categories: 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
