The structure of the native cardiac thin filament troponin core in Ca2+-bound fully activated state 2 from the lower strand. Determined by electron microscopy at 5.8 Å resolution. Released 6 Mar 2024.
Explore 8V0I in 3D Show helices and sheets RCSB PDB PDBe
8V0I contains 62 α-helices and 46 β-strands across 7 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 | 6-7 | 2 | |
| β-strand | 8 | 1 | 1 |
| β-strand | 11 | 1 | 2 |
| β-strand | 17-19 | 3 | 2 |
| β-strand | 21 | 1 | 1 |
| β-strand | 29-31 | 3 | 2 |
| β-strand | 35-38 | 4 | 3 |
| β-strand | 53-54 | 2 | 3 |
| α-helix | 55-59 | 5 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 3 |
| β-strand | 71 | 1 | 4 |
| β-strand | 76 | 1 | 4 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-94 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 5 |
| β-strand | 160-166 | 7 | 5 |
| β-strand | 169-170 | 2 | 5 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 5 |
| α-helix | 182-192 | 11 | |
| α-helix | 193-195 | 3 | |
| α-helix | 205-216 | 12 | |
| α-helix | 223-230 | 8 | |
| β-strand | 238-242 | 5 | 6 |
| β-strand | 245-250 | 6 | 6 |
| α-helix | 258-261 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-295 | 6 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 338-347 | 10 | |
| α-helix | 351-354 | 4 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-369 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-9 | 7 | |
| α-helix | 15-28 | 14 | |
| α-helix | 38-47 | 10 | |
| α-helix | 54-61 | 8 | |
| α-helix | 74-81 | 8 | |
| α-helix | 82-84 | 3 | |
| α-helix | 94-104 | 11 | |
| β-strand | 112 | 1 | 13 |
| α-helix | 114-124 | 11 | |
| α-helix | 130-140 | 11 | |
| β-strand | 148 | 1 | 13 |
| α-helix | 150-156 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 45-79 | 35 | |
| α-helix | 91-133 | 43 | |
| α-helix | 134-138 | 5 | |
| α-helix | 152-159 | 8 | |
| β-strand | 160 | 1 | 14 |
| β-strand | 162 | 1 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 197-211 | 15 | |
| α-helix | 223-266 | 44 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 135-214 | 80 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha cardiac muscle 1 | A, B | protein | 377 | Sus scrofa | A0A8W4F696 (AlphaFold model) |
| Troponin C, slow skeletal and cardiac muscles | C | protein | 161 | Sus scrofa | P63317 (AlphaFold model) |
| Troponin I, cardiac muscle | D | protein | 211 | Sus scrofa | A0A4X1V520 (AlphaFold model) |
| Troponin T2, cardiac type | E | protein | 285 | Sus scrofa | A0A5G2Q8N0 (AlphaFold model) |
| Tropomyosin alpha-1 chain | F, G | protein | 284 | Sus scrofa | P42639 |
>8V0I_1 Actin, alpha cardiac muscle 1 (chains A, B) MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV LSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIS KQEYDEAGPSIVHRKCF
>8V0I_2 Troponin C, slow skeletal and cardiac muscles (chains C) MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEM IDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLEELKIM LQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
>8V0I_3 Troponin I, cardiac muscle (chains D) MADRSGDAAGDSRPAPAPVRRRSSANYRAYATEPHAKKKSKISASRKLQLKTLMLQIAKQ ELEREAEERRGEKGRALSTRCQPLELAGLSFAELQDLCRQLHARVDKVDEERYDVEAKVT KNITEIADLNQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKETLDLRAHLKQVKKE DTEKENREVGDWRKNIDALSGMEGRKKKFEG
>8V0I_4 Troponin T2, cardiac type (chains E) MSDVEETVDEYEEEQEEGAAEEQEEAVEEEAGGEAEAEEANAEEAGQEEDGREAEDGPME ESKPKPRLFMPNLVPPKIPDGERVDFDDIHRKRMKDLNELQTLIEAHFENRKKEEELVSL KDRIEKRRAERAEQQRIRTEREKERQTRLAEERARREEEENRRKAEDEARKKKALSNMMH FGGYIQKQAQTERKSGKRQTEREKKKKILAERRKVLAIDHLNEDQLREKAKELWQSIYNL EAEKFDLQEKFKQQKYEINVLRNRINDNQKVSKTRGKAKVTGRWK
>8V0I_5 Tropomyosin alpha-1 chain (chains F, G) MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKRLEDELVSLQKKLKATEDELDKY SEAPKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAE ERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE FAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Troponin Structural Dynamics in the Native Cardiac Thin Filament Revealed by Cryo Electron Microscopy. Risi, C.M., Belknap, B., Atherton, J. et al. J Mol Biol (2024) 436:168498-168498. DOI 10.1016/j.jmb.2024.168498 · PubMed
Other PDB entries of the same protein (UniProt A0A8W4F696 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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