4pke | pdb_00004pke

The structure of a conserved Piezo channel domain reveals a novel beta sandwich fold

spinqualitylabelsall models 4pke, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pke is a 1 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: PT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PIEZ1_CAEEL Pore-forming subunit of a mechanosensitive non-specific cation channel (By similarity). Generates currents characterized by a linear current-voltage relationship (By similarity). Plays a role in reproduction by positively regulating inter-tissue signaling to promote oocyte maturation, ovulation and fertilization, and sperm navigation from and to the spermatheca (PubMed:32490809). May play a role in regulating cytosolic and endoplasmic reticulum calcium ion release (PubMed:32490809).[UniProtKB:Q92508] Publication Abstract from PubMed Piezo has recently been identified as a family of eukaryotic mechanosensitive channels composed of subunits containing over 2,000 amino acids, without recognizable sequence similarity to other channels. Here, we present the crystal structure of a large, conserved extramembrane domain located just before the last predicted transmembrane helix of C. elegans PIEZO, which adopts a topologically distinct beta sandwich fold. The structure was also determined of a point mutation located on a conserved surface at the position equivalent to the human PIEZO1 mutation found in dehydrated hereditary stomatocytosis patients (M2225R). While the point mutation does not change the overall domain structure, it does alter the surface electrostatic potential that may perturb interactions with a yet-to-be-identified ligand or protein. The lack of structural similarity between this domain and any previously characterized fold, including those of eukaryotic and bacterial channels, highlights the distinctive nature of the Piezo family of eukaryotic mechanosensitive channels. The Structure of a Conserved Piezo Channel Domain Reveals a Topologically Distinct beta Sandwich Fold.,Kamajaya A, Kaiser JT, Lee J, Reid M, Rees DC Structure. 2014 Sep 17. pii: S0969-2126(14)00254-8. doi:, 10.1016/j.str.2014.08.009. PMID:25242456 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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