the Curved Structure of mPIEZO1 in Lipid Bilayer. Determined by electron microscopy at 3.46 Å resolution. Released 13 Apr 2022.
Explore 7WLT in 3D Show helices and sheets RCSB PDB PDBe
7WLT contains 183 α-helices and 48 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 785-823 | 39 | |
| α-helix | 827-839 | 13 | |
| α-helix | 846-867 | 22 | |
| α-helix | 925-949 | 25 | |
| α-helix | 974-984 | 11 | |
| α-helix | 990-1005 | 16 | |
| α-helix | 1008-1022 | 15 | |
| α-helix | 1026-1052 | 27 | |
| α-helix | 1074-1079 | 6 | |
| α-helix | 1094-1113 | 20 | |
| α-helix | 1149-1159 | 11 | |
| α-helix | 1162-1175 | 14 | |
| α-helix | 1181-1200 | 20 | |
| α-helix | 1203-1227 | 25 | |
| α-helix | 1228-1231 | 4 | |
| α-helix | 1243-1249 | 7 | |
| α-helix | 1264-1266 | 3 | |
| α-helix | 1281-1298 | 18 | |
| α-helix | 1300-1364 | 65 | |
| α-helix | 1403-1407 | 5 | |
| α-helix | 1412-1415 | 4 | |
| α-helix | 1494-1547 | 54 | |
| α-helix | 1553-1556 | 4 | |
| α-helix | 1657-1668 | 12 | |
| α-helix | 1673-1685 | 13 | |
| α-helix | 1687-1700 | 14 | |
| α-helix | 1705-1713 | 9 | |
| α-helix | 1714-1718 | 5 | |
| α-helix | 1727-1748 | 22 | |
| α-helix | 1759-1762 | 4 | |
| α-helix | 1770-1774 | 5 | |
| α-helix | 1787-1802 | 16 | |
| α-helix | 1947-1967 | 21 | |
| α-helix | 1977-1996 | 20 | |
| α-helix | 2017-2040 | 24 | |
| α-helix | 2043-2059 | 17 | |
| α-helix | 2060-2064 | 5 | |
| α-helix | 2065-2068 | 4 | |
| α-helix | 2077-2099 | 23 | |
| α-helix | 2101-2102 | 2 | |
| α-helix | 2109-2111 | 3 | |
| α-helix | 2116-2127 | 12 | |
| α-helix | 2131-2142 | 12 | |
| α-helix | 2149-2174 | 26 | |
| α-helix | 2182-2184 | 3 | |
| α-helix | 2185-2213 | 29 | |
| β-strand | 2219 | 1 | 1 |
| β-strand | 2223-2232 | 10 | 2 |
| β-strand | 2236-2243 | 8 | 2 |
| β-strand | 2248-2250 | 3 | 3 |
| α-helix | 2251-2252 | 2 | |
| α-helix | 2253-2262 | 10 | |
| α-helix | 2267-2275 | 9 | |
| α-helix | 2278-2280 | 3 | |
| β-strand | 2281-2284 | 4 | 3 |
| β-strand | 2286-2287 | 2 | 4 |
| α-helix | 2298-2309 | 12 | |
| β-strand | 2315-2325 | 11 | 2 |
| β-strand | 2335-2344 | 10 | 2 |
| α-helix | 2349-2357 | 9 | |
| β-strand | 2366-2372 | 7 | 5 |
| β-strand | 2375-2378 | 4 | 3 |
| α-helix | 2385 | 1 | |
| β-strand | 2386 | 1 | 3 |
| α-helix | 2387 | 1 | |
| β-strand | 2399-2409 | 11 | 5 |
| α-helix | 2423-2425 | 3 | |
| β-strand | 2426-2434 | 9 | 5 |
| β-strand | 2443-2444 | 2 | 4 |
| β-strand | 2447-2450 | 4 | 3 |
| β-strand | 2453 | 1 | 1 |
| α-helix | 2467-2482 | 16 | |
| α-helix | 2489-2492 | 4 | |
| α-helix | 2501-2516 | 16 | |
| α-helix | 2519-2534 | 16 | |
| α-helix | 2536-2542 | 7 | |
| α-helix | 2545-2546 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Piezo-type mechanosensitive ion channel component 1 | A, C, E | protein | 2547 | Mus musculus | E2JF22 (AlphaFold model) |
>7WLT_1 Piezo-type mechanosensitive ion channel component 1 (chains A, C, E) MEPHVLGAGLYWLLLPCTLLAASLLRFNALSLVYLLFLLLLPWLPGPSRHSIPGHTGRLL RALLCLSLLFLVAHLAFQICLHTVPHLDQFLGQNGSLWVKVSQHIGVTRLDLKDIFNTTR LVAPDLGVLLASSLCLGLCGRLTRKAGQSRRTQELQDDDDDDDDDDEDIDAAPAVGLKGA PALATKRRLWLASRFRVTAHWLLMTSGRTLVIVLLALAGIAHPSAFSSIYLVVFLAICTW WSCHFPLSPLGFNTLCVMVSCFGAGHLICLYCYQTPFIQDMLPPGNIWARLFGLKNFVDL PNYSSPNALVLNTKHAWPIYVSPGILLLLYYTATSLLKLHKSCPSELRKETPREDEEHEL ELDHLEPEPQARDATQGEMPMTTEPDLDNCTVHVLTSQSPVRQRPVRPRLAELKEMSPLH GLGHLIMDQSYVCALIAMMVWSIMYHSWLTFVLLLWACLIWTVRSRHQLAMLCSPCILLY GLTLCCLRYVWAMELPELPTTLGPVSLHQLGLEHTRYPCLDLGAMLLYLLTFWLLLRQFV KEKLLKKQKVPAALLEVTVADTEPTQTQTLLRSLGELVTGIYVKYWIYVCAGMFIVVSFA GRLVVYKIVYMFLFLLCLTLFQVYYTLWRKLLRVFWWLVVAYTMLVLIAVYTFQFQDFPT YWRNLTGFTDEQLGDLGLEQFSVSELFSSILIPGFFLLACILQLHYFHRPFMQLTDLEHV PPPGTRHPRWAHRQDAVSEAPLLEHQEEEEVFREDGQSMDGPHQATQVPEGTASKWGLVA DRLLDLAASFSAVLTRIQVFVRRLLELHVFKLVALYTVWVALKEVSVMNLLLVVLWAFAL PYPRFRPMASCLSTVWTCIIIVCKMLYQLKIVNPHEYSSNCTEPFPNNTNLQPLEINQSL LYRGPVDPANWFGVRKGYPNLGYIQNHLQILLLLVFEAVVYRRQEHYRRQHQQAPLPAQA VCADGTRQRLDQDLLSCLKYFINFFFYKFGLEICFLMAVNVIGQRMNFMVILHGCWLVAI LTRRRREAIARLWPNYCLFLTLFLLYQYLLCLGMPPALCIDYPWRWSKAIPMNSALIKWL YLPDFFRAPNSTNLISDFLLLLCASQQWQVFSAERTEEWQRMAGINTDHLEPLRGEPNPI PNFIHCRSYLDMLKVAVFRYLFWLVLVVVFVAGATRISIFGLGYLLACFYLLLFGTTLLQ KDTRAQLVLWDCLILYNVTVIISKNMLSLLSCVFVEQMQSNFCWVIQLFSLVCTVKGYYD PKEMMTRDRDCLLPVEEAGIIWDSICFFFLLLQRRIFLSHYFLHVSADLKATALQASRGF ALYNAANLKSINFHRQIEEKSLAQLKRQMKRIRAKQEKYRQSQASRGQLQSKDPQDPSQE PGPDSPGGSSPPRRQWWRPWLDHATVIHSGDYFLFESDSEEEEEALPEDPRPAAQSAFQM AYQAWVTNAQTVLRQRRERARQERAEQLASGGDLNPDVEPVDVPEDEMAGRSHMMQRVLS TMQFLWVLGQATVDGLTRWLRAFTKHHRTMSDVLCAERYLLTQELLRVGEVRRGVLDQLY VGEDEATLSGPVETRDGPSTASSGLGAEEPLSSMTDDTSSPLSTGYNTRSGSEEIVTDAG DLQAGTSLHGSQELLANARTRMRTASELLLDRRLHIPELEEAERFEAQQGRTLRLLRAGY QCVAAHSELLCYFIIILNHMVTASAASLVLPVLVFLWAMLTIPRPSKRFWMTAIVFTEVM VVTKYLFQFGFFPWNSYVVLRRYENKPYFPPRILGLEKTDSYIKYDLVQLMALFFHRSQL LCYGLWDHEEDRYPKDHCRSSVKDREAKEEPEAKLESQSETGTGHPKEPVLAGTPRDHIQ GKGSIRSKDVIQDPPEDLKPRHTRHISIRFRRRKETPGPKGTAVMETEHEEGEGKETTER KRPRHTQEKSKFRERMKAAGRRLQSFCVSLAQSFYQPLQRFFHDILHTKYRAATDVYALM FLADIVDIIIIIFGFWAFGKHSAATDIASSLSDDQVPQAFLFMLLVQFGTMVIDRALYLR KTVLGKLAFQVVLVVAIHIWMFFILPAVTERMFSQNAVAQLWYFVKCIYFALSAYQIRCG YPTRILGNFLTKKYNHLNLFLFQGFRLVPFLVELRAVMDWVWTDTTLSLSNWMCVEDIYA NIFIIKCSRETEKKYPQPKGQKKKKIVKYGMGGLIILFLIAIIWFPLLFMSLIRSVVGVV NQPIDVTVTLKLGGYEPLFTMSAQQPSIVPFTPQAYEELSQQFDPYPLAMQFISQYSPED IVTAQIEGSSGALWRISPPSRAQMKQELYNGTADITLRFTWNFQRDLAKGGTVEYTNEKH TLELAPNSTARRQLAQLLEGRPDQSVVIPHLFPKYIRAPNGPEANPVKQLQPDEEEDYLG VRIQLRREQVGTGASGEQAGTKASDFLEWWVIELQDCKADCNLLPMVIFSDKVSPPSLGF LAGYGIVGLYVSIVLVVGKFVRGFFSEISHSIMFEELPCVDRILKLCQDIFLVRETRELE LEEELYAKLIFLYRSPETMIKWTRERE
| ID | Name | Formula | Copies |
|---|---|---|---|
| P5S | O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine | C42 H82 N O10 P | 3 |
| PEE | 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine | C41 H78 N O8 P | 3 |
| PLX | (9R,11S)-9-({[(1S)-1-hydroxyhexadecyl]oxy}methyl)-2,2-dimethyl-5,7,10-trioxa-2L… | C42 H89 N O8 P | 21 |
Structure deformation and curvature sensing of PIEZO1 in lipid membranes. Yang, X., Lin, C., Chen, X. et al. Nature (2022) 604:377-383. DOI 10.1038/s41586-022-04574-8 · PubMed
Other PDB entries of the same protein (UniProt E2JF22 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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