2gdx
Solution structure of the B. brevis TycC3-PCP in H-state
OverviewOverview
Protein dynamics plays an important role in protein function. Many functionally important motions occur on the microsecond and low millisecond time scale and can be characterized by nuclear magnetic resonance relaxation experiments. We describe the different states of a peptidyl carrier protein (PCP) that play a crucial role in its function as a peptide shuttle in the nonribosomal peptide synthetases of the tyrocidine A system. Both apo-PCP (without the bound 4'-phosphopantetheine cofactor) and holo-PCP exist in two different stable conformations. We show that one of the apo conformations and one of the holo conformations are identical, whereas the two remaining conformations are only detectable by nuclear magnetic resonance spectroscopy in either the apo or holo form. We further demonstrate that this conformational diversity is an essential prerequisite for the directed movement of the 4'-PP cofactor and its interaction with externally acting proteins such as thioesterases and 4'-PP transferase.
About this StructureAbout this Structure
2GDX is a Single protein structure of sequence from Brevibacillus parabrevis. Full crystallographic information is available from OCA.
ReferenceReference
Conformational switches modulate protein interactions in peptide antibiotic synthetases., Koglin A, Mofid MR, Lohr F, Schafer B, Rogov VV, Blum MM, Mittag T, Marahiel MA, Bernhard F, Dotsch V, Science. 2006 Apr 14;312(5771):273-6. PMID:16614225 Page seeded by OCA on Sun May 4 04:59:49 2008