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Literature summary for 2.7.11.7 extracted from

  • Ye, Q.; Crawley, S.W.; Yang, Y.; Cote, G.P.; Jia, Z.
    Crystal structure of the alpha-kinase domain of Dictyostelium myosin heavy chain kinase A (2010), Sci. Signal., 3, ra17.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.7

Crystallization (Commentary)

Crystallization (Comment) Organism
MHCK A in complex with ATP and a peptide substrate, and MHCK A alpha kinase domain in individual complexes with AMP, ADP, and beta,gamma-methyleneadenosine 5'-triphosphate, X-ray diffraction structcure determination and analysis Dictyostelium discoideum

Protein Variants

Protein Variants Comment Organism
D766A site-directed mutagenesis of the central active site residue, inactive mutant Dictyostelium discoideum
D766E site-directed mutagenesis of the central active site residue, inactive mutant Dictyostelium discoideum
D766S site-directed mutagenesis of the central active site residue, inactive mutant Dictyostelium discoideum
K645A site-directed mutagenesis of an alpha-kinase domain residue, the mutant shows 98.5% reduced activity compared to the wild-type enzyme Dictyostelium discoideum
R592A site-directed mutagenesis of an alpha-kinase domain residue, the mutant shows 92% reduced activity compared to the wild-type enzyme Dictyostelium discoideum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, Mg2+ is coordinated in an octahedral arrangement by the side chains of Asp766 and Gln768, the main-chain carbonyl group of Pro767, and three water molecules Dictyostelium discoideum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
130000
-
 MHCK A Dictyostelium discoideum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [myosin heavy-chain] Dictyostelium discoideum
-
 ADP + [myosin heavy-chain] phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Dictyostelium discoideum P42527
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [myosin heavy-chain]
-
 Dictyostelium discoideum ADP + [myosin heavy-chain] phosphate
-
 ?
ATP + [myosin heavy-chain] phosphorylation of sites within the MHC alpha-helical, coiled-coil tail by MHCK A Dictyostelium discoideum ADP + [myosin heavy-chain] phosphate
-
 ?
additional information the enzyme also exhibits ATPase and unspecific Ser/Thr protein kinase activities Dictyostelium discoideum ?
-
 ?

Subunits

Subunits Comment Organism
More MHCK A protein consists of an N-terminal coiled-coil domain, a central kinase domain, and a C-terminal WD-repeat domain, domain structures comparisons of the catalytic alpha-kinase domain to the one from Mus musculus, overview Dictyostelium discoideum

Synonyms

Synonyms Comment Organism
MHCK A
-
 Dictyostelium discoideum
myosin heavy chain kinase A
-
 Dictyostelium discoideum

Cofactor

Cofactor Comment Organism Structure
ATP binds to the catalytic alpha-kinase domain Dictyostelium discoideum

General Information

General Information Comment Organism
evolution alpha-kinases transfer the gamma-phosphate of ATP to protein substrates through an aspartylphosphate intermediate Dictyostelium discoideum
additional information ADP is bound at the active site and invariant Asp766 at the active site is phosphorylated in the crysstallized MHCK A. The aspartylphosphate group is exposed to the solvent within an active-site pocket that might function as a docking site for substrates. Access to the aspartylphosphate is regulated by a conformational switch in a loop that binds to a Mg2+ ion, providing a mechanism that allows alpha-kinases to sense and respond to local changes in Mg2+ concentration. Access to the active-site pocket was regulated by a C-terminal glycine-rich loop that bound to Mg2+ and switched between two distinct conformations. The invariant Asp766 residue is located at the center rear of the active site where it interacted with phosphate, the alpha-phosphate of AMP, and Mg2+ in the active-site pocket Dictyostelium discoideum
physiological function myosin II heavy chain kinase A, MHCK A, disrupts the assembly and cellular activity of bipolar filaments of myosin II by phosphorylating sites within its alpha-helical, coiled-coil tail Dictyostelium discoideum