PDBsum entry 4ttp

Transferase

PDB id: 4ttp

Contents

Protein chain

201 a.a.

Waters ×91

PDB id:

4ttp

Name:

Transferase

Title:

Crystal structure of legionella pneumophila dephospho-coa kinase in apo-form

Structure:

Dephospho-coa kinase. Chain: a. Synonym: dephosphocoenzyme a kinase. Engineered: yes

Source:

Legionella pneumophila subsp. Pneumophila. Organism_taxid: 272624. Strain: philadelphia 1 / atcc 33152 / dsm 7513. Gene: coae, lpg1467. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å R-factor: 0.190 R-free: 0.220

Authors:

X.Gong,H.Ge

Key ref:

X.Gong et al. (2014). Crystal structure of Legionella pneumophila dephospho-CoA kinase reveals a non-canonical conformation of P-loop. J Struct Biol, 188, 233-239. PubMed id: 25449315 DOI: 10.1016/j.jsb.2014.10.008

Date:

22-Jun-14 Release date: 10-Dec-14

Protein chain

Q5ZVH3  (COAE_LEGPH) -  Dephospho-CoA kinase from Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)

Seq: 201 a.a.

Struc: 201 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.1.24 - dephospho-CoA kinase.
• Pathway: Coenzyme A Biosynthesis (late stages)
• Reaction: 3'-dephospho-CoA + ATP = ADP + CoA + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.jsb.2014.10.008

J Struct Biol 188:233-239 (2014)

PubMed id: 25449315

Crystal structure of Legionella pneumophila dephospho-CoA kinase reveals a non-canonical conformation of P-loop.

X.Gong, X.Chen, D.Yu, N.Zhang, Z.Zhu, L.Niu, Y.Mao, H.Ge.

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.