9GIX: Mitochondrial pyruvate carrier 1-like protein

Structure of the human mitochondrial pyruvate carrier in the apo-state. Determined by electron microscopy at 3.65 Å resolution. Released 7 May 2025.

Method: Electron microscopy
Resolution: 3.65 Å
Organisms: Homo sapiens, synthetic construct
Chains: 3
Atoms: 2,733
Mol. weight: 86.56 kDa
Released: 7 May 2025

Explore 9GIX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9GIX contains 16 α-helices and 13 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.

Chain A: 7 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	7-16	10
α-helix	18-25	8
α-helix	27-35	9
α-helix	37-46	10
α-helix	50-52	3
α-helix	55-74	20
β-strand	76	1	1
α-helix	80-106	27

Chain B: 5 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	9-21	13
α-helix	29-33	5
α-helix	41-60	20
α-helix	69-88	20
β-strand	90	1	1
α-helix	94-120	27

Chain C: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	2
β-strand	13-14	2	3
β-strand	21-28	8	2
α-helix	30-35	6
α-helix	37-39	3
β-strand	41-47	7	3
β-strand	53-59	7	3
β-strand	66-68	3	3
β-strand	76-81	6	2
β-strand	86-91	6	2
α-helix	96-98	3
β-strand	100-107	8	3
α-helix	115-117	3
β-strand	120-121	2	3
β-strand	125-128	4	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitochondrial pyruvate carrier 1-like protein	A	protein	136	Homo sapiens	P0DKB6 (AlphaFold model)
Mitochondrial pyruvate carrier 2	B	protein	133	Homo sapiens	O95563 (AlphaFold model)
MBP-nanobody,Maltose/maltodextrin-binding periplasmic protein	C	protein	515	synthetic construct	P0AEY0 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9GIX_1 Mitochondrial pyruvate carrier 1-like protein (chains A)
MARMAVLWRKMRDNFQSKEFREYVSSTHFWGPAFSWGLPLAAFKDMKASPEIISGRMTTA
LILYSAIFMRFAYRVQPRNLLLMACHCTNVMAQSVQASRYLLYYYGGGGAEAKARDPPAT
AAAATSPGSQPPKQAS

Sequence of entity 2 (B), FASTA

>9GIX_2 Mitochondrial pyruvate carrier 2 (chains B)
MSAAGARGLRATYHRLLDKVELMLPEKLRPLYNHPAGPRTVFFWAPIMKWGLVCAGLADM
ARPAEKLSTAQSAVLMATGFIWSRYSLVIIPKNWSLFAVNFFVGAAGASQLFRIWRYNQE
LKAKAHKENLYFQ

Sequence of entity 3 (C), FASTA

>9GIX_3 MBP-nanobody,Maltose/maltodextrin-binding periplasmic protein (chains C)
GPSQVQLVESGGGLVQAGGSLRLSCAASGRTFSAYGISTYTMGWFRQAPGKEREFVAAIG
RDSGFTYYEDSVKGRFTINADNAENTVYLQMNSLKPEDTAVYYCAASSYYGRPNVDLMAY
WGKGTQVTVPPLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGD
GPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSL
IYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGK
YDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNI
DTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNK
DKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQ
TVDEALKDAQTPGSPDAAIEGRTSEDAWSHPQFEK

Primary citation

Molecular basis of pyruvate transport and inhibition of the human mitochondrial pyruvate carrier. Sichrovsky, M., Lacabanne, D., Ruprecht, J.J. et al. Sci Adv (2025) 11:eadw1489-eadw1489. DOI 10.1126/sciadv.adw1489 · PubMed

Other PDB entries of the same protein (UniProt P0DKB6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9GIV 3.65 Å, Structure of the human mitochondrial pyruvate carrier inhibited by a UK5099-derivative
9GIY 3.79 Å, Structure of the human mitochondrial pyruvate carrier inhibited by mitoglitazone
9GIW 3.92 Å, Structure of the human mitochondrial pyruvate carrier inhibited by zaprinast

Browse structure collections

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