7BTY: Mitochondrial outer membrane beta-barrel protein

The mitochondrial SAM-Mdm10 supercomplex in Nanodisc from S.cere. Determined by electron microscopy at 3.2 Å resolution. Released 20 Jan 2021.

Method: Electron microscopy
Resolution: 3.2 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 10,168
Mol. weight: 172.46 kDa
Released: 20 Jan 2021

Explore 7BTY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7BTY contains 47 α-helices and 69 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: 4 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	126-129	4	1
β-strand	139-146	8	1
β-strand	156-166	11	1
β-strand	169-181	13	1
β-strand	184-196	13	1
α-helix	198-201	4
β-strand	204-216	13	1
β-strand	235-250	16	1
α-helix	264-269	6
β-strand	271-285	15	1
β-strand	297-306	10	1
β-strand	310-322	13	1
β-strand	330-342	13	1
α-helix	350-352	3
β-strand	357	1	2
β-strand	376	1	3
β-strand	381	1	3
β-strand	384	1	2
β-strand	386-395	10	1
β-strand	408-420	13	1
α-helix	428-434	7
β-strand	441-449	9	1
β-strand	454-462	9	1
β-strand	464-466	3	4
β-strand	474-480	7	1

Chain B: 19 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	21-23	3	4
α-helix	34-40	7
β-strand	41-42	2	5
β-strand	45	1	6
β-strand	60-64	5	5
β-strand	67-69	3	7
β-strand	75	1	8
β-strand	76-78	3	7
α-helix	81-93	13
β-strand	97	1	6
α-helix	98-99	2
β-strand	100	1	8
β-strand	115-117	3	5
α-helix	120-122	3
β-strand	130-133	4	5
β-strand	139-141	3	5
α-helix	143-151	9
α-helix	159-166	8
α-helix	167-171	5
α-helix	172-180	9
α-helix	185-191	7
α-helix	204-215	12
α-helix	218-224	7
α-helix	230-233	4
α-helix	235-239	5
α-helix	248-271	24
α-helix	272-274	3
α-helix	282-283	2
α-helix	286-296	11
α-helix	305-311	7
α-helix	314-324	11

Chain C: 19 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	9
α-helix	20-30	11
α-helix	35-39	5
β-strand	46-47	2	9
α-helix	52-54	3
β-strand	62-65	4	9
β-strand	69-72	4	9
α-helix	74-83	10
α-helix	105-107	3
α-helix	108-117	10
α-helix	118-122	5
α-helix	123-127	5
α-helix	128-132	5
α-helix	134-136	3
α-helix	137-141	5
α-helix	157-168	12
α-helix	204-206	3
α-helix	208-226	19
α-helix	228-240	13
α-helix	252-264	13
α-helix	268-279	12
α-helix	281-295	15
β-strand	304-305	2	9
α-helix	317-323	7

Chain L: 5 helices, 31 β-strands

Element	Residues	Length	Sheet
α-helix	5-16	12
α-helix	20-22	3
α-helix	30-33	4
α-helix	37-40	4
β-strand	44-52	9	10
β-strand	55-62	8	10
β-strand	68-76	9	10
α-helix	82-86	5
β-strand	140-147	8	10
β-strand	152	1	10
β-strand	155-159	5	10
β-strand	166	1	10
β-strand	168-174	7	10
β-strand	179-189	11	10
β-strand	194-199	6	10
β-strand	206	1	10
β-strand	209-210	2	11
β-strand	230-231	2	12
β-strand	234-238	5	11
β-strand	239	1	10
β-strand	247-251	5	11
β-strand	254-255	2	12
β-strand	258	1	13
β-strand	263	1	13
β-strand	271	1	11
β-strand	282-284	3	14
β-strand	292-294	3	14
β-strand	310	1	14
β-strand	313	1	10
β-strand	317	1	15
β-strand	412	1	15
β-strand	413-421	9	10
β-strand	426-434	9	10
β-strand	438-447	10	10
β-strand	481-486	6	10
β-strand	488-491	4	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitochondrial outer membrane beta-barrel protein	A	protein	363	Saccharomyces cerevisiae	E9P977 (AlphaFold model)
Sorting assembly machinery 35 kDa subunit	B	protein	329	Saccharomyces cerevisiae	P14693 (AlphaFold model)
Sorting assembly machinery 37 kDa subunit	C	protein	327	Saccharomyces cerevisiae	P50110 (AlphaFold model)
MDM10 isoform 1	L	protein	493	Saccharomyces cerevisiae	A0A6A5PXD8

Sequence of entity 1 (A), FASTA

>7BTY_1 Mitochondrial outer membrane beta-barrel protein (chains A)
TFTAKTGTNFGNDNDAEAYLQFEKLIDKKYLKLPTRVNLEILRGTKIHSSFLFNSYSSLS
PQSILNLKVFSQFYNWNTNKGLDIGQRGARLSLRYEPLFLHKLLHNPHSNESPTLFHEWF
LETCWRSTKICSQGTSAPYMYSGTMLSQAGDQLRTILGHTFVLDKRDHIMCPTKGSMLKW
SNELSPGKHLKTQLELNSVKSWMNDDFITFSTTIKTGYLKNLSSQQSLPVHICDKFQSGG
PSDIRGFQTFGLGPRDLYDAVGGDAFVSYGLSVFSRLPWKKVEKSNFRLHWFFNGGKLVN
HDNTSLGNCIGQLSKEHSTSTGIGLVLRHPMARFELNFTLPITAHENDLIRKGFQFGLGL
AFL

Sequence of entity 2 (B), FASTA

>7BTY_2 Sorting assembly machinery 35 kDa subunit (chains B)
MVSSFSVPMPVKRIFDTFPLQTYAAQTDKDEAVALEIQRRSYTFTERGGGSSELTVEGTY
KLGVYNVFLEANTGAALATDPWCLFVQLALCQKNGLVLPTHSQEQTPSHTCNHEMLVLSR
LSNPDEALPILVEGYKKRIIRSTVAISEIMRSRILDDAEQLMYYTLLDTVLYDCWITQII
FCASDAQFMELYSCQKLSGSIVTPLDVENSLLQKLSAKSLKISLTKRNKFQFRHREIVKS
MQGVYHNHHNSVNQEQVLNVLFENSKQVLLGLKDMLKSDGQPTYLHLKIASYILCITNVK
EPIKLKTFVENECKELVQFAQDTLKNFVQ

Sequence of entity 3 (C), FASTA

>7BTY_3 Sorting assembly machinery 37 kDa subunit (chains C)
MVKGSVHLWGKDGKASLISVDSIALVWFIKLCTSEEAKSMVAGLQIVFSNNTDLSSDGKL
PVLILDNGTKVSGYVNIVQFLHKNICTSKYEKGTDYEEDLAIVRKKDRLLEYSLLNYVDV
EISRLTDYQLFLNTKNYNEYTKKLFSKLLYFPMWYNTPLQLRSQARENCEEIIGSLTLED
DEEFVESKAMESASQLAQSKTFKIAHKNKIKGKQELQQVKYNLQFDNRLQSCVSNWLAAR
KKLDDSVILSSDLLFLANLYVQLGLPDGNRIRSKLEQTFGSELLNSMSNKIDDFVHRPSN
NLEQRDPQFREQGNVVMSLYNLACKYI

Sequence of entity 4 (L), FASTA

>7BTY_4 MDM10 isoform 1 (chains L)
MLPYMDQVLRAFYQSTHWSTQNSYEDITATSRTLLDFRIPSAIHLQISNKSTPNTFNSLD
FSTRSRINGSLSYLYSDAQQLEKFMRNSTDIPLQDATETYRQLQPNLNFSVSSANTLSSD
NTTVDNDKKLLHDSKFVKKSLYYGRMYYPSSDLEAMIIKRLSPQTQFMLKGVSSFKESLN
VLTCYFQRDSHRNLQEWIFSTSDLLCGYRVLHNFLTTPSKFNTSLYNNSSLSLGAEFWLG
LVSLSPGCSTTLRYYTHSTNTGRPLTLTLSWNPLFGHISSTYSAKTGTNSTFCAKYDFNL
YSIESNLSFGCEFWQKKHHLLETNKNNNDKLEPISDELVDINPNSRATKLLHENVPDLNS
AVNDIPSTLDIPVHKQKLLNDLTYAFSSSLRKIDEERSTIEKFDNKINSSIFTSVWKLST
SLRDKTLKLLWEGKWRGFLISAGTELVFTRGFQESLSDDEKNDNAISISATDTENGNIPV
FPAKFGIQFQYST

Primary citation

Mitochondrial sorting and assembly machinery operates by beta-barrel switching. Takeda, H., Tsutsumi, A., Nishizawa, T. et al. Nature (2021) 590:163-169. DOI 10.1038/s41586-020-03113-7 · PubMed

Other PDB entries of the same protein (UniProt E9P977 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7BTX 2.8 Å, The mitochondrial SAM-Mdm10 supercomplex in GDN micelle from S.cere
7BTW 2.9 Å, The mitochondrial SAM complex from S.cere

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