7ED9
Crystal structure of selenomethionine-labeled Thermus thermophilus FakA ATP-binding domain
Summary for 7ED9
| Entry DOI | 10.2210/pdb7ed9/pdb |
| Descriptor | Probable kinase, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | fatty acid kinase, atp-binding protein, lipid metabolism, phosphotransferase, biosynthetic protein |
| Biological source | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
| Total number of polymer chains | 2 |
| Total formula weight | 48347.18 |
| Authors | Nakatani, M.,Nakahara, S.,Fukui, K.,Murakawa, T.,Masui, R. (deposition date: 2021-03-15, release date: 2022-03-16, Last modification date: 2023-11-29) |
| Primary citation | 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 Cited by 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: 36228973DOI: 10.1016/j.jsb.2022.107904 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01764160944 Å) |
Structure validation
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