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PDBsum entry 4ttp
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References listed in PDB file
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Key reference
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Title
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Crystal structure of legionella pneumophila dephospho-Coa kinase reveals a non-Canonical conformation of p-Loop.
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Authors
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X.Gong,
X.Chen,
D.Yu,
N.Zhang,
Z.Zhu,
L.Niu,
Y.Mao,
H.Ge.
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Ref.
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J Struct Biol, 2014,
188,
233-239.
[DOI no: ]
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PubMed id
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Abstract
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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.
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