6LVU

Crystal structure of apo acyl carrier protein from Thermotoga maritima

Summary for 6LVU

• Entry DOI: 10.2210/pdb6lvu/pdb
• Descriptor: Acyl carrier protein, ZINC ION (3 entities in total)
• Functional Keywords: acyl carrier protein, biosynthetic protein
• Biological source: Thermotoga maritima MSB8
• Total number of polymer chains: 2
• Total formula weight: 18400.66

Authors

Lee, Y.,Lee, W.C.,Kim, Y. (deposition date: 2020-02-05, release date: 2020-04-22, Last modification date: 2023-11-29)

Primary citation

Lee, Y.,Jang, A.,Jeong, M.C.,Park, N.,Park, J.,Lee, W.C.,Cheong, C.,Kim, Y.
Structural Characterization of an ACP fromThermotoga maritima: Insights into Hyperthermal Adaptation.
Int J Mol Sci, 21:-, 2020

PubMed Abstract: , a deep-branching hyperthermophilic bacterium, expresses an extraordinarily stable acyl carrier protein (-ACP) that functions as a carrier in the fatty acid synthesis system at near-boiling aqueous environments. Here, to understand the hyperthermal adaptation of -ACP, we investigated the structure and dynamics of -ACP by nuclear magnetic resonance (NMR) spectroscopy. The melting temperature of -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 cell membrane. -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 -ACP. Our findings provide insights into the structural basis of the hyperthermal adaptation of ACP, which might have allowed to survive in hot ancient oceans.

PubMed: 32283632
DOI: 10.3390/ijms21072600

Experimental method

X-RAY DIFFRACTION (2.294 Å)