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Structural Characterization of an ACP from Thermotoga maritima: Insights into Hyperthermal Adaptation.


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.

SUBMITTER: Lee Y 

PROVIDER: S-EPMC7178038 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature

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Structural Characterization of an ACP from <i>Thermotoga maritima</i>: Insights into Hyperthermal Adaptation.

Lee Yeongjoon Y   Jang Ahjin A   Jeong Min-Cheol MC   Park Nuri N   Park Jungwoo J   Lee Woo Cheol WC   Cheong Chaejoon C   Kim Yangmee Y  

International journal of molecular sciences 20200409 7


<i>Thermotoga maritima</i>, a deep-branching hyperthermophilic bacterium, expresses an extraordinarily stable <i>Thermotoga maritima</i> acyl carrier protein (<i>Tm</i>-ACP) that functions as a carrier in the fatty acid synthesis system at near-boiling aqueous environments. Here, to understand the hyperthermal adaptation of <i>Tm</i>-ACP, we investigated the structure and dynamics of <i>Tm</i>-ACP by nuclear magnetic resonance (NMR) spectroscopy. The melting temperature of <i>Tm</i>-ACP (101.4 °  ...[more]

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