2GDW

Solution structure of the B. brevis TycC3-PCP in A/H-state

Summary for 2GDW

• Entry DOI: 10.2210/pdb2gdw/pdb
• Related: 2GDX 2GDY 2GE0 2GE1
• Descriptor: Tyrocidine synthetase III (1 entity in total)
• Functional Keywords: three-helix bundle, ligase-transport protein complex, ligase/transport protein
• Biological source: Brevibacillus parabrevis
• Total number of polymer chains: 1
• Total formula weight: 9250.68

Authors

Koglin, A.,Loehr, F.,Rogov, V.V.,Marahiel, M.A.,Bernhard, F.,Doetsch, V. (deposition date: 2006-03-17, release date: 2006-08-01, Last modification date: 2024-05-29)

Primary citation

Koglin, A.,Mofid, M.R.,Loehr, F.,Schaefer, B.,Rogov, V.V.,Blum, M.-M.,Mittag, T.,Marahiel, M.A.,Bernhard, F.,Doetsch, V.
Conformational switches modulate protein interactions in peptide antibiotic synthetases
Science, 312:273-276, 2006

PubMed Abstract: 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.

PubMed: 16614225
DOI: 10.1126/science.1122928

Experimental method

SOLUTION NMR