PMID:25449315

Citation	Gong, X, Chen, X, Yu, D, Zhang, N, Zhu, Z, Niu, L, Mao, Y and Ge, H (2014) Crystal structure of Legionella pneumophila dephospho-CoA kinase reveals a non-canonical conformation of P-loop. J. Struct. Biol. 188:233-9
Abstract	Dephospho-CoA kinase (DPCK; EC 2.7.1.24) catalyzes the final step in the coenzyme A biosynthetic pathway. DPCK transfers a phosphate group from ATP to the 3-hydroxyl group of the ribose of dephosphocoenzyme A (dCoA) to yield CoA and ADP. Upon the binding of ligands, large conformational changes is induced in DPCKs, as well as in many other kinases, to shield the bound ATP in their catalytic site from the futile hydrolysis by bulk water molecules. To investigate the molecular mechanisms underlying the phosphoryl transfer during DPCK catalytic cycle, we determined the crystal structures of the Legionellapneumophila DPCK (LpDPCK) both in its apo-form and in complex with ATP. The structures reveal that LpDPCK comprises of three domains, the classical core domain, the CoA domain, and the LID domain, which are packed together to create a central cavity for substrate-binding and enzymatic catalysis. The binding of ATP induces large conformational changes, including a hinge-bending motion of the CoA binding domain and the "helix to loop" conformational change of the P-loop. Finally, modeling of a dCoA molecule to the enzyme provides insights into the catalytic mechanism of DPCK.
Links	PubMed Online version:10.1016/j.jsb.2014.10.008
Keywords	Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Legionella pneumophila/metabolism; Models, Molecular; Phosphotransferases (Alcohol Group Acceptor)/metabolism; Protein Conformation
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
LEGPH:COAE		GO:0004140: dephospho-CoA kinase activity	ECO:0000314:		F		Dephosphocoenzyme A kinase (DPCK; CoaE) catalyses the phosphorylation of the 3′-hydroxyl group of the ribose moiety of dephospho-CoA.	complete CACAO 11514
LEGPH:COAE		GO:0004140: dephospho-CoA kinase activity	ECO:0000255:	PMID:25449315	F		Structure of Lp-DPCK-Bu2 was determined by molecular replacement with Phaser	complete CACAO 11916

References

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