Ontology highlight
ABSTRACT:
SUBMITTER: Yang X
PROVIDER: S-EPMC10978961 | biostudies-literature | 2024 Mar
REPOSITORIES: biostudies-literature
Yang Xiaoke X Zhu Mingqi M Lu Xue X Wang Yuxin Y Xiao Junyu J
Nature communications 20240328 1
The study of phosphorylase kinase (PhK)-regulated glycogen metabolism has contributed to the fundamental understanding of protein phosphorylation; however, the molecular mechanism of PhK remains poorly understood. Here we present the high-resolution cryo-electron microscopy structures of human muscle PhK. The 1.3-megadalton PhK α<sub>4</sub>β<sub>4</sub>γ<sub>4</sub>δ<sub>4</sub> hexadecamer consists of a tetramer of tetramer, wherein four αβγδ modules are connected by the central β<sub>4</sub> ...[more]