3LLA

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

3LLA の概要

• エントリーDOI: 10.2210/pdb3lla/pdb
• 関連するPDBエントリー: 3LKM 3LMH 3LMI
• 分子名称: Myosin heavy chain kinase A, ZINC ION, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ... (5 entities in total)
• 機能のキーワード: protein kinase like fold, atp-binding, kinase, nucleotide-binding, serine/threonine-protein kinase, alpha-kinase, coiled coil, wd repeat, transferase
• 由来する生物種: Dictyostelium discoideum (Slime mold)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70384.34

構造登録者

Ye, Q.,Jia, Z. (登録日: 2010-01-28, 公開日: 2010-03-16, 最終更新日: 2023-09-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.11 Å)