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Dynamics in an unusual acyl carrier protein (ACP) from a ladderane lipid-synthesizing organism

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Dietl,  Andreas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Barends,  Thomas R.M.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Dietl, A., & Barends, T. R. (2022). Dynamics in an unusual acyl carrier protein (ACP) from a ladderane lipid-synthesizing organism. Proteins: Structure, Function, and Bioinformatics, 90(1), 73-82. doi:10.1002/prot.26187.


Cite as: http://hdl.handle.net/21.11116/0000-0008-F383-1
Abstract
Anaerobic ammonium-oxidizing (anammox) bacteria express a distinct acyl carrier protein implicated in the biosynthesis of the highly unusual "ladderane" lipids these organisms produce. This "anammox-specific" ACP, or amxACP, shows several unique features such as a conserved FF motif and an unusual sequence in the functionally important helix III. Investigation of the protein's structure and dynamics, both in the crystal by ensemble refinement and by MD simulations reveal that helix III adopts a rare six-residue-long 310 -helical conformation that confers a large degree of conformational and positional variability on this part of the protein. This way of introducing structural flexibility by using the inherent properties of 310 -helices appears unique among ACPs. Moreover, the structure suggests a role for the FF motif in shielding the thioester linkage between the protein's prosthetic group and its acyl cargo from hydrolysis. This article is protected by copyright. All rights reserved.