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TitleCryo-EM Structure of a KCNQ1/CaM Complex Reveals Insights into Congenital Long QT Syndrome.
Journal, issue, pagesCell, Vol. 169, Issue 6, Page 1042-11050.e9, Year 2017
Publish dateJun 1, 2017
AuthorsJi Sun / Roderick MacKinnon /
PubMed AbstractKCNQ1 is the pore-forming subunit of cardiac slow-delayed rectifier potassium (I) channels. Mutations in the kcnq1 gene are the leading cause of congenital long QT syndrome (LQTS). Here, we present ...KCNQ1 is the pore-forming subunit of cardiac slow-delayed rectifier potassium (I) channels. Mutations in the kcnq1 gene are the leading cause of congenital long QT syndrome (LQTS). Here, we present the cryoelectron microscopy (cryo-EM) structure of a KCNQ1/calmodulin (CaM) complex. The conformation corresponds to an "uncoupled," PIP-free state of KCNQ1, with activated voltage sensors and a closed pore. Unique structural features within the S4-S5 linker permit uncoupling of the voltage sensor from the pore in the absence of PIP. CaM contacts the KCNQ1 voltage sensor through a specific interface involving a residue on CaM that is mutated in a form of inherited LQTS. Using an electrophysiological assay, we find that this mutation on CaM shifts the KCNQ1 voltage-activation curve. This study describes one physiological form of KCNQ1, depolarized voltage sensors with a closed pore in the absence of PIP, and reveals a regulatory interaction between CaM and KCNQ1 that may explain CaM-mediated LQTS.
External linksCell / PubMed:28575668 / PubMed Central
MethodsEM (single particle)
Resolution3.7 Å
Structure data

EMDB-8712, PDB-5vms:
CryoEM structure of Xenopus KCNQ1 channel
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • xenopus laevis (African clawed frog)
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / CALCIUM BINDING PROTEIN / KCNQ1-CaM complex / potassium channel / Long QT syndrome

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