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TitleArchitecture and activation of human muscle phosphorylase kinase.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 2719, Year 2024
Publish dateMar 28, 2024
AuthorsXiaoke Yang / Mingqi Zhu / Xue Lu / Yuxin Wang / Junyu Xiao /
PubMed AbstractThe study of phosphorylase kinase (PhK)-regulated glycogen metabolism has contributed to the fundamental understanding of protein phosphorylation; however, the molecular mechanism of PhK remains ...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 αβγδ hexadecamer consists of a tetramer of tetramer, wherein four αβγδ modules are connected by the central β scaffold. The α- and β-subunits possess glucoamylase-like domains, but exhibit no detectable enzyme activities. The α-subunit serves as a bridge between the β-subunit and the γδ subcomplex, and facilitates the γ-subunit to adopt an autoinhibited state. Ca-free calmodulin (δ-subunit) binds to the γ-subunit in a compact conformation. Upon binding of Ca, a conformational change occurs, allowing for the de-inhibition of the γ-subunit through a spring-loaded mechanism. We also reveal an ADP-binding pocket in the β-subunit, which plays a role in allosterically enhancing PhK activity. These results provide molecular insights of this important kinase complex.
External linksNat Commun / PubMed:38548794 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.1 Å
Structure data

36212

8jfk

EMDB-36212, PDB-8jfk:
PhK holoenzyme in inactive state, muscle isoform
Method: EM (single particle) / Resolution: 2.9 Å

36213

8jfl

EMDB-36213, PDB-8jfl:
PhK holoenzyme in active state, muscle isoform
Method: EM (single particle) / Resolution: 2.9 Å

36214

8xya

EMDB-36214: local map of hPhK alpha-beta-gamma-delta subcomplex in inactive state
PDB-8xya: hPhK alpha-beta-gamma-delta subcomplex in inactive state
Method: EM (single particle) / Resolution: 2.7 Å

36215

8xyb

EMDB-36215: local map of hPhK gamma-delta subcomplex in inactive state
PDB-8xyb: hPhK gamma-delta subcomplex in inactive state
Method: EM (single particle) / Resolution: 3.1 Å

36216

8xy7

EMDB-36216: local map of hPhK alpha-gamma subcomplex in active state
PDB-8xy7: hPhK alpha-gamma subcomplex in active state
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-FAR:
FARNESYL / Farnesol

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • homo sapiens (human)
KeywordsCYTOSOLIC PROTEIN / glycogen phosphorylase b kinase / muscle isoform / inactive state / Ca2+ active state / hPhK alpha-gamma subcomplex / alpha-beta-gamma-delta subcomplex / gamma-delta subcomplex

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