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PDBsum entry 5e4h
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PDB id:
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Transferase
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Title:
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Crystal structure of apoenzyme alpha-kinase domain of myosin-ii heavy chain kinase a
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Structure:
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Myosin-ii heavy chain kinase a. Chain: a, b, c, d, e, f, g, h. Fragment: alpha kinase domain (unp residues 552-841). Synonym: mhck-a. Engineered: yes
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Source:
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Dictyostelium discoideum. Slime mold. Organism_taxid: 44689. Gene: mhka, mhcka, ddb_g0291231. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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2.90Å
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R-factor:
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0.242
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R-free:
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0.268
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Authors:
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Q.Ye,G.P.Cote,Z.Jia
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Key ref:
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Q.Ye
et al.
(2016).
Structure of the Dictyostelium Myosin-II Heavy Chain Kinase A (MHCK-A) α-kinase domain apoenzyme reveals a novel autoinhibited conformation.
Sci Rep,
6,
26634.
PubMed id:
DOI:
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Date:
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06-Oct-15
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Release date:
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08-Jun-16
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PROCHECK
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Headers
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References
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P42527
(MHCKA_DICDI) -
Myosin heavy chain kinase A from Dictyostelium discoideum
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Seq:
Struc:
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1146 a.a.
252 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Enzyme class:
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E.C.2.7.11.7
- [myosin heavy-chain] kinase.
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Reaction:
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L-threonyl-[myosin heavy-chain] + ATP = O-phospho-L-threonyl-[myosin heavy-chain] + ADP + H+
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L-threonyl-[myosin heavy-chain]
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+
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ATP
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=
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O-phospho-L-threonyl-[myosin heavy-chain]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Sci Rep
6:26634
(2016)
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PubMed id:
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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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Q.Ye,
Y.Yang,
L.van Staalduinen,
S.W.Crawley,
L.Liu,
S.Brennan,
G.P.Côté,
Z.Jia.
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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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