PDBsum entry 5e9e

Transferase

PDB id: 5e9e

Contents

Protein chains

255 a.a.

Ligands

ANP ×2

PO4 ×2

Metals

_ZN ×2

Waters ×213

PDB id:

5e9e

Name:

Transferase

Title:

Crystal structure of the alpha-kinase domain of myosin-ii heavy chain kinase a in complex with amp-pnp

Structure:

Myosin-ii heavy chain kinase a. Chain: a, b. Fragment: alpha kinase domain (unp residues 552-841). Synonym: mhck-a. Engineered: yes

Source:

Dictyostelium discoideum. Slime mold. Organism_taxid: 44689. Gene: mhka, mhcka, ddb_g0291231. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.40Å R-factor: 0.194 R-free: 0.236

Authors:

Q.Ye,Z.Jia

Key ref:

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: 27211275 DOI: 10.1038/srep26634

Date:

15-Oct-15 Release date: 08-Jun-16

Protein chains

P42527  (MHCKA_DICDI) -  Myosin heavy chain kinase A from Dictyostelium discoideum

Seq: 1146 a.a.

Struc: 255 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.7 - [myosin heavy-chain] kinase.
• Reaction: L-threonyl-[myosin heavy-chain] + ATP = O-phospho-L-threonyl-[myosin heavy-chain] + ADP + H⁺

L-threonyl-[myosin heavy-chain] + ATP = O-phospho-L-threonyl-[myosin heavy-chain] (Bound ligand (Het Group name = ANP) matches with 81.25% similarity) + ADP + H(+)

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

Added reference

DOI no: 10.1038/srep26634

Sci Rep 6:26634 (2016)

PubMed id: 27211275

Structure of the Dictyostelium Myosin-II Heavy Chain Kinase A (MHCK-A) α-kinase domain apoenzyme reveals a novel autoinhibited conformation.

Q.Ye, Y.Yang, L.van Staalduinen, S.W.Crawley, L.Liu, S.Brennan, G.P.Côté, Z.Jia.

ABSTRACT

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.