3LLA

Crystal Structure of the Alpha-kinase Domain of Myosin Heavy Chain Kinase A Complex with AMPPCP

Summary for 3LLA

• Entry DOI: 10.2210/pdb3lla/pdb
• Related: 3LKM 3LMH 3LMI
• Descriptor: Myosin heavy chain kinase A, ZINC ION, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ... (5 entities in total)
• Functional Keywords: protein kinase like fold, atp-binding, kinase, nucleotide-binding, serine/threonine-protein kinase, alpha-kinase, coiled coil, wd repeat, transferase
• Biological source: Dictyostelium discoideum (Slime mold)
• Total number of polymer chains: 2
• Total formula weight: 70384.34

Authors

Ye, Q.,Jia, Z. (deposition date: 2010-01-28, release date: 2010-03-16, Last modification date: 2023-09-06)

Primary citation

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.
Sci.Signal., 3:ra17-ra17, 2010

PubMed Abstract: Dictyostelium discoideum 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. MHCK A is a member of the atypical alpha-kinase family of serine and threonine protein kinases and displays no sequence homology to typical eukaryotic protein kinases. We report the crystal structure of the alpha-kinase domain (A-CAT) of MHCK A. When crystallized in the presence of adenosine triphosphate (ATP), A-CAT contained adenosine monophosphate (AMP) at the active site. However, when crystallized in the presence of ATP and a peptide substrate, which does not appear in the structure, adenosine diphosphate (ADP) was found at the active site and an invariant aspartic acid residue (Asp(766)) at the active site was phosphorylated. The aspartylphosphate group was exposed to the solvent within an active-site pocket that might function as a docking site for substrates. Access to the aspartylphosphate was regulated by a conformational switch in a loop that bound to a magnesium ion (Mg(2+)), providing a mechanism that allows alpha-kinases to sense and respond to local changes in Mg(2+).

PubMed: 20197546
DOI: 10.1126/scisignal.2000525

Experimental method

X-RAY DIFFRACTION (2.11 Å)