6YTX

Cryo-EM structure of undecameric human CALHM6 in the presence of Ca2+


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 6.23 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Cryo-EM structures and functional properties of CALHM channels of the human placenta.

Drozdzyk, K.Sawicka, M.Bahamonde-Santos, M.I.Jonas, Z.Deneka, D.Albrecht, C.Dutzler, R.

(2020) Elife 9

  • DOI: https://doi.org/10.7554/eLife.55853
  • Primary Citation of Related Structures:  
    6YTK, 6YTL, 6YTO, 6YTQ, 6YTV, 6YTX

  • PubMed Abstract: 

    The transport of substances across the placenta is essential for the development of the fetus. Here, we were interested in the role of channels of the calcium homeostasis modulator (CALHM) family in the human placenta. By transcript analysis, we found the paralogs CALHM2, 4, and 6 to be highly expressed in this organ and upregulated during trophoblast differentiation. Based on electrophysiology, we observed that activation of these paralogs differs from the voltage- and calcium-gated channel CALHM1. Cryo-EM structures of CALHM4 display decameric and undecameric assemblies with large cylindrical pore, while in CALHM6 a conformational change has converted the pore shape into a conus that narrows at the intracellular side, thus describing distinct functional states of the channel. The pore geometry alters the distribution of lipids, which occupy the cylindrical pore of CALHM4 in a bilayer-like arrangement whereas they have redistributed in the conical pore of CALHM6 with potential functional consequences.


  • Organizational Affiliation

    Department of Biochemistry, University of Zurich, Zurich, Switzerland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Calcium homeostasis modulator protein 6
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J, K
315Homo sapiensMutation(s): 0 
Gene Names: CALHM6C6orf187FAM26F
Membrane Entity: Yes 
UniProt & NIH Common Fund Data Resources
Find proteins for Q5R3K3 (Homo sapiens)
Explore Q5R3K3 
Go to UniProtKB:  Q5R3K3
PHAROS:  Q5R3K3
GTEx:  ENSG00000188820 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5R3K3
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 6.23 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Swiss National Science Foundation--

Revision History  (Full details and data files)

  • Version 1.0: 2020-05-13
    Type: Initial release
  • Version 1.1: 2020-05-20
    Changes: Database references