7ED9

Crystal structure of selenomethionine-labeled Thermus thermophilus FakA ATP-binding domain

7ED9 の概要

• エントリーDOI: 10.2210/pdb7ed9/pdb
• 分子名称: Probable kinase, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: fatty acid kinase, atp-binding protein, lipid metabolism, phosphotransferase, biosynthetic protein
• 由来する生物種: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48347.18

構造登録者

Nakatani, M.,Nakahara, S.,Fukui, K.,Murakawa, T.,Masui, R. (登録日: 2021-03-15, 公開日: 2022-03-16, 最終更新日: 2023-11-29)

主引用文献

Nakatani, M.,Nakahara, S.Y.,Fukui, K.,Urano, M.,Fujii, Y.,Murakawa, T.,Baba, S.,Kumasaka, T.,Okanishi, H.,Kanai, Y.,Yano, T.,Masui, R.
Crystal structure of a nucleotide-binding domain of fatty acid kinase FakA from Thermus thermophilus HB8.
J.Struct.Biol., 214:107904-107904, 2022

PubMed Abstract: Fatty acid kinase is necessary for the incorporation of exogenous fatty acids into membrane phospholipids. Fatty acid kinase consists of two components: a kinase component, FakA, that phosphorylates a fatty acid bound to a fatty acid-binding component, FakB. However, the molecular details underlying the phosphotransfer reaction remain to be resolved. We determined the crystal structure of the N-terminal domain of FakA bound to ADP from Thermus thermophilus HB8. The overall structure of this domain showed that the helical barrel fold is similar to the nucleotide-binding component of dihydroxyacetone kinase. The structure of the nucleotide-binding site revealed the roles of the conserved residues in recognition of ADP and Mg, but the N-terminal domain of FakA lacked the ADP-capping loop found in the dihydroxyacetone kinase component. Based on the structural similarity to the two subunits of dihydroxyacetone kinase complex, we constructed a model of the complex of T. thermophilus FakB and the N-terminal domain of FakA. In this model, the invariant Arg residue of FakB occupied a position that was spatially similar to that of the catalytically important Arg residue of dihydroxyacetone kinase, which predicted a composite active site in the Fatty acid kinase complex.

PubMed: 36228973
DOI: 10.1016/j.jsb.2022.107904

実験手法

X-RAY DIFFRACTION (2.01764160944 Å)