6lmt | pdb_00006lmt

Cryo-EM structure of the killifish CALHM1

spinqualitylabelsall models 6lmt, resolution 2.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6lmt is a 8 chain structure with sequence from Japanese killifish. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Y01 Gene: CALHM1 (Japanese killifish) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Calcium homeostasis modulator (CALHM) family proteins are Ca(2+)-regulated adenosine triphosphate (ATP)-release channels involved in neural functions including neurotransmission in gustation. Here, we present the cryo-electron microscopy (EM) structures of killifish CALHM1, human CALHM2, and Caenorhabditis elegans CLHM-1 at resolutions of 2.66, 3.4, and 3.6 A, respectively. The CALHM1 octamer structure reveals that the N-terminal helix forms the constriction site at the channel pore in the open state and modulates the ATP conductance. The CALHM2 undecamer and CLHM-1 nonamer structures show the different oligomeric stoichiometries among CALHM homologs. We further report the cryo-EM structures of the chimeric construct, revealing that the intersubunit interactions at the transmembrane domain (TMD) and the TMD-intracellular domain linker define the oligomeric stoichiometry. These findings advance our understanding of the ATP conduction and oligomerization mechanisms of CALHM channels. Cryo-EM structures of calcium homeostasis modulator channels in diverse oligomeric assemblies.,Demura K, Kusakizako T, Shihoya W, Hiraizumi M, Nomura K, Shimada H, Yamashita K, Nishizawa T, Taruno A, Nureki O Sci Adv. 2020 Jul 17;6(29):eaba8105. doi: 10.1126/sciadv.aba8105. eCollection, 2020 Jul. PMID:32832629 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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