2ge0 | pdb_00002ge0

ACTIVE COMPLEX OF COENZYME A AND THE PPTASE SFP FROM B. SUBTILIS

spinqualitylabelsall models 2ge0 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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