5DYJ

Mysosin heavy chain kinase A catalytic domain mutant - D663A

5DYJ の概要

• エントリーDOI: 10.2210/pdb5dyj/pdb
• 分子名称: Myosin heavy chain kinase A, PHOSPHATE ION, ZINC ION, ... (6 entities in total)
• 機能のキーワード: kinase, 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: 70236.13

構造登録者

van Staalduinen, L.M.,Yang, Y.,Jia, Z. (登録日: 2015-09-24, 公開日: 2016-06-08, 最終更新日: 2024-10-23)

主引用文献

Ye, Q.,Yang, Y.,van Staalduinen, L.,Crawley, S.W.,Liu, L.,Brennan, S.,Cote, G.P.,Jia, Z.
Structure of the Dictyostelium Myosin-II Heavy Chain Kinase A (MHCK-A) alpha-kinase domain apoenzyme reveals a novel autoinhibited conformation.
Sci Rep, 6:26634-26634, 2016

PubMed 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.

PubMed: 27211275
DOI: 10.1038/srep26634

実験手法

X-RAY DIFFRACTION (2.5 Å)