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

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.

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 Creators:
Dietl, Andreas1, Author              
Barends, Thomas R.M.1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: ACP; acyl carrier protein; ensemble refinement; lipid biosynthesis; molecular dynamics; protein dynamics
 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.

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Language(s): eng - English
 Dates: 2020-11-182021-07-162021-07-262022-01
 Publication Status: Published in print
 Pages: 22
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 Table of Contents: -
 Rev. Type: Peer
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Title: Proteins: Structure, Function, and Bioinformatics
Source Genre: Journal
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Publ. Info: New York, NY : John Wiley & Sons
Pages: - Volume / Issue: 90 (1) Sequence Number: - Start / End Page: 73 - 82 Identifier: ISSN: 0887-3585
CoNE: https://pure.mpg.de/cone/journals/resource/954925553393_1