8YW9: Mitochondrial pyruvate carrier 2

Cryo-EM structure of human mitochondrial pyruvate carrier in the matrix-facing conformation at pH 6.8. Determined by electron microscopy at 3.01 Å resolution. Released 12 Mar 2025.

Method
Electron microscopy
Resolution
3.01 Å
Organisms
Homo sapiens, Escherichia coli BL21(DE3)
Chains
4
Atoms
3,709
Mol. weight
61.69 kDa
Ligands
CDL
Released
12 Mar 2025

Explore 8YW9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8YW9 contains 18 α-helices and 24 β-strands across 4 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.

Chain A: 7 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix17-226
α-helix25-339
α-helix35-428
α-helix43-453
α-helix48-503
α-helix53-7220
α-helix78-10730
Chain B: 7 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix6-2318
α-helix29-324
α-helix41-477
α-helix50-589
α-helix59-613
α-helix69-8820
α-helix94-12532
Chain C: 1 helix, 13 β-strands
ElementResiduesLengthSheet
β-strand3-751
β-strand10-1342
β-strand17-2591
β-strand34-3962
β-strand45-5172
β-strand58-6032
β-strand68-7361
β-strand78-8471
α-helix88-903
β-strand92-9872
β-strand102-10433
β-strand107-10933
β-strand116-11722
β-strand121-12662
Chain D: 3 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand3-754
β-strand10-1235
β-strand18-2584
β-strand34-3965
β-strand46-5165
β-strand58-6035
α-helix62-643
β-strand68-7364
α-helix74-763
β-strand78-8364
α-helix88-903
β-strand92-9875
β-strand104-10525
β-strand109-11355

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Mitochondrial pyruvate carrier 2Bprotein151Homo sapiensO95563 (AlphaFold model)
Mitochondrial pyruvate carrier 1Aprotein120Homo sapiensQ9Y5U8 (AlphaFold model)
MPC specific nanobody 2Cprotein127Escherichia coli BL21(DE3)
MPC specific nanobody 1Dprotein138Escherichia coli BL21(DE3)
Sequence of entity 1 (B), FASTA
>8YW9_1 Mitochondrial pyruvate carrier 2 (chains B)
MSAAGARGLRATYHRLLDKVELMLPEKLRPLYNHPAGPRTVFFWAPIMKWGLVCAGLADM
ARPAEKLSTAQSAVLMATGFIWSRYSLVIIPKNWSLFAVNFFVGAAGASQLFRIWRYNQE
LKAKAHKGSDYKDHDGDYKDHDIDYKDDDDK
Sequence of entity 2 (A), FASTA
>8YW9_2 Mitochondrial pyruvate carrier 1 (chains A)
MAGALVRKAADYVRSKDFRDYLMSTHFWGPVANWGLPIAAINDMKKSPEIISGRMTFALC
CYSLTFMRFAYKVQPRNWLLFACHATNEVAQLIQGGRLIKHEMTKTASAGSYPYDVPDYA
Sequence of entity 3 (C), FASTA
>8YW9_3 MPC specific nanobody 2 (chains C)
EVQLVESGGGLVQAGGSLRLSCAASGITYRHYAIGWFRQAPGKEREGVARIRSSTGQTYY
ADSVKGRFTMSRDNSKNTVYLQMNSLKPEDTALYYCAYGPLYYYEGGWAWPNYYDYWGQG
TQVTVSS
Sequence of entity 4 (D), FASTA
>8YW9_4 MPC specific nanobody 1 (chains D)
EVQLVESGGGLVQAGGSLRLSCAASGFPVTERVMYWYRQAPGKEREWVAAIDSQGSSTYY
ADSVKGRFTISRDNSKNTVYLQMNSLKPEDTAVYYCKVEVGWGYKGQGTQVTVSSLEHHH
HHHHGGSGEQKLISEEDL

Ligands and cofactors

IDNameFormulaCopies
CDLCardiolipinC81 H156 O17 P21

Primary citation

Structures and mechanism of the human mitochondrial pyruvate carrier. Liang, J., Shi, J., Song, A. et al. Nature (2025) 641:258-265. DOI 10.1038/s41586-025-08873-8 · PubMed

Other PDB entries of the same protein (UniProt O95563 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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