Structural Characterization of an ACP from <i>Thermotoga maritima</i>: Insights into Hyperthermal Adaptation
<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 env...
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2020-04-01
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| Series: | International Journal of Molecular Sciences |
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| author | Yeongjoon Lee Ahjin Jang Min-Cheol Jeong Nuri Park Jungwoo Park Woo Cheol Lee Chaejoon Cheong Yangmee Kim |
| author_facet | Yeongjoon Lee Ahjin Jang Min-Cheol Jeong Nuri Park Jungwoo Park Woo Cheol Lee Chaejoon Cheong Yangmee Kim |
| author_sort | Yeongjoon Lee |
| collection | DOAJ |
| description | <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 °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 <i>T. maritima</i> cell membrane. <i>Tm</i>-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 <i>Tm</i>-ACP. Our findings provide insights into the structural basis of the hyperthermal adaptation of ACP, which might have allowed <i>T. maritima</i> to survive in hot ancient oceans. |
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| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T20:35:05Z |
| publishDate | 2020-04-01 |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-20832c9e3c844469935b0a091f8db5172023-11-19T21:05:18ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-04-01217260010.3390/ijms21072600Structural Characterization of an ACP from <i>Thermotoga maritima</i>: Insights into Hyperthermal AdaptationYeongjoon Lee0Ahjin Jang1Min-Cheol Jeong2Nuri Park3Jungwoo Park4Woo Cheol Lee5Chaejoon Cheong6Yangmee Kim7Department of Bioscience and Biotechnology, Konkuk University, Seoul 05029, KoreaDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 05029, KoreaDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 05029, KoreaDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 05029, KoreaDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 05029, KoreaDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 05029, KoreaMagnetic Resonance Team, Korea Basic Science Institute, Ochang 28199, KoreaDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Korea<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 °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 <i>T. maritima</i> cell membrane. <i>Tm</i>-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 <i>Tm</i>-ACP. Our findings provide insights into the structural basis of the hyperthermal adaptation of ACP, which might have allowed <i>T. maritima</i> to survive in hot ancient oceans.https://www.mdpi.com/1422-0067/21/7/2600Acyl carrier proteinNMR spectroscopystructurethermostability<i>Thermotoga maritima</i> |
| spellingShingle | Yeongjoon Lee Ahjin Jang Min-Cheol Jeong Nuri Park Jungwoo Park Woo Cheol Lee Chaejoon Cheong Yangmee Kim Structural Characterization of an ACP from <i>Thermotoga maritima</i>: Insights into Hyperthermal Adaptation International Journal of Molecular Sciences Acyl carrier protein NMR spectroscopy structure thermostability <i>Thermotoga maritima</i> |
| title | Structural Characterization of an ACP from <i>Thermotoga maritima</i>: Insights into Hyperthermal Adaptation |
| title_full | Structural Characterization of an ACP from <i>Thermotoga maritima</i>: Insights into Hyperthermal Adaptation |
| title_fullStr | Structural Characterization of an ACP from <i>Thermotoga maritima</i>: Insights into Hyperthermal Adaptation |
| title_full_unstemmed | Structural Characterization of an ACP from <i>Thermotoga maritima</i>: Insights into Hyperthermal Adaptation |
| title_short | Structural Characterization of an ACP from <i>Thermotoga maritima</i>: Insights into Hyperthermal Adaptation |
| title_sort | structural characterization of an acp from i thermotoga maritima i insights into hyperthermal adaptation |
| topic | Acyl carrier protein NMR spectroscopy structure thermostability <i>Thermotoga maritima</i> |
| url | https://www.mdpi.com/1422-0067/21/7/2600 |
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