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- Title
Structural Characterization of an ACP from Thermotoga maritima: Insights into Hyperthermal Adaptation.
- Authors
Lee, Yeongjoon; Jang, Ahjin; Jeong, Min-Cheol; Park, Nuri; Park, Jungwoo; Lee, Woo Cheol; Cheong, Chaejoon; Kim, Yangmee
- Abstract
Thermotoga maritima, a deep-branching hyperthermophilic bacterium, expresses an extraordinarily stable Thermotoga maritima acyl carrier protein (Tm-ACP) that functions as a carrier in the fatty acid synthesis system at near-boiling aqueous environments. Here, to understand the hyperthermal adaptation of Tm-ACP, we investigated the structure and dynamics of Tm-ACP by nuclear magnetic resonance (NMR) spectroscopy. The melting temperature of Tm-ACP (101.4 °C) far exceeds that of other ACPs, owing to extensive ionic interactions and tight hydrophobic packing. The D59 residue, which replaces Pro/Ser of other ACPs, mediates ionic clustering between helices III and IV. This creates a wide pocket entrance to facilitate the accommodation of long acyl chains required for hyperthermal adaptation of the T. maritima cell membrane. Tm-ACP is revealed to be the first ACP that harbor an amide proton hyperprotected against hydrogen/deuterium exchange for I15. The hydrophobic interactions mediated by I15 appear to be the key driving forces of the global folding process of Tm-ACP. Our findings provide insights into the structural basis of the hyperthermal adaptation of ACP, which might have allowed T. maritima to survive in hot ancient oceans.
- Subjects
THERMOTOGA maritima; ACYL carrier protein; NUCLEAR magnetic resonance spectroscopy; NUCLEAR magnetic resonance; HYDROPHOBIC interactions; IONIC interactions
- Publication
International Journal of Molecular Sciences, 2020, Vol 21, Issue 7, p2600
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms21072600