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PDBsum entry 5e4h
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References listed in PDB file
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Key reference
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Title
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Structure of the dictyostelium myosin-Ii heavy chain kinase a (mhck-A) α-Kinase domain apoenzyme reveals a novel autoinhibited conformation.
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Authors
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Q.Ye,
Y.Yang,
L.Van staalduinen,
S.W.Crawley,
L.Liu,
S.Brennan,
G.P.Côté,
Z.Jia.
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Ref.
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Sci Rep, 2016,
6,
26634.
[DOI no: ]
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PubMed id
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Abstract
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The α-kinases are a family of a typical protein kinases present in organisms
ranging from protozoa to mammals. Here we report an autoinhibited conformation
for the α-kinase domain of Dictyostelium myosin-II heavy chain kinase A
(MHCK-A) in which nucleotide binding to the catalytic cleft, located at the
interface between an N-terminal and C-terminal lobe, is sterically blocked by
the side chain of a conserved arginine residue (Arg592). Previous α-kinase
structures have shown that an invariant catalytic aspartic acid residue (Asp766)
is phosphorylated. Unexpectedly, in the autoinhibited conformation the
phosphoryl group is transferred to the adjacent Asp663, creating an interaction
network that stabilizes the autoinhibited state. The results suggest that Asp766
phosphorylation may play both catalytic and regulatory roles. The autoinhibited
structure also provides the first view of a phosphothreonine residue docked into
the phospho-specific allosteric binding site (Pi-pocket) in the C-lobe of the
α-kinase domain.
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