| RRC ID |
73677
|
| Author |
Nakatani M, Nakahara SY, Fukui K, Urano M, Fujii Y, Murakawa T, Baba S, Kumasaka T, Okanishi H, Kanai Y, Yano T, Masui R.
|
| Title |
Crystal structure of a nucleotide-binding domain of fatty acid kinase FakA from Thermus thermophilus HB8.
|
| Journal |
J Struct Biol
|
| 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 Mg2+, 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.
|
| Volume |
214(4)
|
| Pages |
107904
|
| Published |
2022-12-1
|
| DOI |
10.1016/j.jsb.2022.107904
|
| PII |
S1047-8477(22)00074-0
|
| PMID |
36228973
|
| MeSH |
Adenosine Diphosphate
Fatty Acids*
Thermus thermophilus*
|
| IF |
3.071
|
| Resource |
| DNA material |
TEx08D02 (THR003274)
TEx03D12 (THR001284)
Thermus thermophilus expression plasmid
TEx05B11 (THR002035) |
