5GJW

Structure of the mammalian voltage-gated calcium channel Cav1.1 complex for ClassII map

Summary for 5GJW

• Entry DOI: 10.2210/pdb5gjw/pdb
• Related: 5GJV
• EMDB information: 9514 9515
• Related PRD ID: PRD_900017
• Descriptor: Voltage-dependent L-type calcium channel subunit alpha-1S, CALCIUM ION, Voltage-dependent L-type calcium channel subunit beta-1, ... (10 entities in total)
• Functional Keywords: complex, channel, membrane protein
• Biological source: Oryctolagus cuniculus (Rabbit); More
• Total number of polymer chains: 5
• Total formula weight: 402198.60

Authors

Wu, J.P.,Yan, Z.,Li, Z.Q.,Zhou, Q.,Yan, N. (deposition date: 2016-07-02, release date: 2016-09-14, Last modification date: 2024-10-23)

Primary citation

Wu, J.P.,Yan, Z.,Li, Z.Q.,Qian, X.Y.,Lu, S.,Dong, M.Q.,Zhou, Q.,Yan, N.
Structure of the voltage-gated calcium channel Cav1.1 at 3.6 angstrom resolution
Nature, 537:191-196, 2016

PubMed Abstract: The voltage-gated calcium (Ca) channels convert membrane electrical signals to intracellular Ca-mediated events. Among the ten subtypes of Ca channel in mammals, Ca1.1 is specified for the excitation-contraction coupling of skeletal muscles. Here we present the cryo-electron microscopy structure of the rabbit Ca1.1 complex at a nominal resolution of 3.6 Å. The inner gate of the ion-conducting α1-subunit is closed and all four voltage-sensing domains adopt an 'up' conformation, suggesting a potentially inactivated state. The extended extracellular loops of the pore domain, which are stabilized by multiple disulfide bonds, form a windowed dome above the selectivity filter. One side of the dome provides the docking site for the α2δ-1-subunit, while the other side may attract cations through its negative surface potential. The intracellular I-II and III-IV linker helices interact with the β-subunit and the carboxy-terminal domain of α1, respectively. Classification of the particles yielded two additional reconstructions that reveal pronounced displacement of β and adjacent elements in α1. The atomic model of the Ca1.1 complex establishes a foundation for mechanistic understanding of excitation-contraction coupling and provides a three-dimensional template for molecular interpretations of the functions and disease mechanisms of Ca and Na channels.

PubMed: 27580036
DOI: 10.1038/nature19321

Experimental method

ELECTRON MICROSCOPY (3.9 Å)