Probing the Phosphopantetheine Arm Conformations of Acyl Carrier Proteins Using Vibrational Spectroscopy
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چکیده
منابع مشابه
Probing the Phosphopantetheine Arm Conformations of Acyl Carrier Proteins Using Vibrational Spectroscopy
Acyl carrier proteins (ACPs) are universal and highly conserved domains central to both fatty acid and polyketide biosynthesis. These proteins tether reactive acyl intermediates with a swinging 4'-phosphopantetheine (Ppant) arm and interact with a suite of catalytic partners during chain transport and elongation while stabilizing the growing chain throughout the biosynthetic pathway. The flexib...
متن کاملCorrection to “Probing the Phosphopantetheine Arm Conformations of Acyl Carrier Proteins Using Vibrational Spectroscopy”
■ REFERENCES (1) Corrected ref 2: Nguyen, C.; Haushalter, R. W.; Lee, D. J.; Markwick, P. R. L.; Bruegger, J.; Caldara-Festin, G.; Finzel, K.; Jackson, D. R.; Ishikawa, F.; O’Dowd, B.; McCammon, J. A.; Opella, S. J.; Tsai, S.-C.; Burkart, M. D. Nature 2014, 505, 427. (2) Corrected ref 3: Masoudi, A.; Raetz, C. R. H.; Zhou, P.; Pemble, C. W., IV. Nature 2014, 505, 422. (3) Corrected ref 4: Dutta...
متن کاملAcyl carrier protein. V. Identification of 4'-phosphopantetheine bound to a mammalian fatty acid synthetase preparation.
Previous investigations from several laboratories have established the sequence of reactions leading to de novo synthesis of fatty acids.'-8 Previous reports have also shown that all these reactions in E. coli occur with the substrates bound as thioesters to an acyl carrier protein (ACP).7-12 Recently, the substrate binding site of ACP has been shown to be the sulfhydryl group of a prosthetic g...
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Vibrational energy relaxation (VER) of a selected mode in cytochrome c (hemeprotein) in vacuum is studied using two theoretical approaches: One is the equilibrium simulation approach with quantum correction factors, and the other is the reduced model approach which describes the protein as an ensemble of normal modes coupled with nonlinear coupling elements. Both methods result in estimates of ...
متن کاملThe function of acyl carrier protein in the synthesis of membrane-derived oligosaccharides does not require its phosphopantetheine prosthetic group.
An enzyme system catalyzing the synthesis of the beta 1,2-linked glucan backbone of the membrane-derived oligosaccharides of Escherichia coli from UDP-glucose has an essential requirement for the E. coli acyl carrier protein (ACP). This finding was surprising, because all other characterized functions of ACP involve acyl thioester residues linked to the phosphopantetheine moiety covalently boun...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2014
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja505442h