7BTW: The mitochondrial SAM complex from S.cere

The mitochondrial SAM complex from S.cere. Determined by electron microscopy at 2.9 Å resolution. Released 20 Jan 2021.

Method: Electron microscopy
Resolution: 2.9 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 10,246
Mol. weight: 157.24 kDa
Released: 20 Jan 2021

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

Secondary structure: helices and β-sheets

7BTW contains 46 α-helices and 61 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, 22 β-strands

Element	Residues	Length	Sheet
β-strand	126-129	4	1
β-strand	138-146	9	1
α-helix	147-148	2
β-strand	156-165	10	1
β-strand	168-181	14	1
β-strand	184-197	14	1
β-strand	203-216	14	1
β-strand	237-251	15	1
α-helix	264-269	6
β-strand	273-283	11	1
β-strand	297-306	10	1
β-strand	310-322	13	1
β-strand	330-341	12	1
α-helix	350-352	3
β-strand	357	1	2
β-strand	368	1	3
β-strand	376	1	4
β-strand	381	1	4
β-strand	384	1	2
β-strand	386-395	10	1
β-strand	408-420	13	1
α-helix	428-433	6
β-strand	439-449	11	1
β-strand	454-465	12	1
β-strand	471	1	3
β-strand	474-478	5	1

Chain B: 19 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	21-22	2	1
α-helix	33-36	4
β-strand	41-42	2	5
α-helix	43-44	2
β-strand	45	1	6
β-strand	60-64	5	5
β-strand	67-69	3	7
β-strand	76-78	3	7
α-helix	81-94	14
β-strand	97	1	6
α-helix	98-100	3
β-strand	115-117	3	5
β-strand	130-133	4	5
β-strand	139-141	3	5
α-helix	143-151	9
α-helix	158-166	9
α-helix	167-171	5
α-helix	172-177	6
α-helix	178-182	5
α-helix	185-192	8
α-helix	204-215	12
α-helix	217-224	8
α-helix	230-233	4
α-helix	235-242	8
α-helix	248-272	25
α-helix	286-296	11
α-helix	304-311	8
α-helix	314-322	9
α-helix	324-326	3

Chain C: 19 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	8
β-strand	11	1	9
β-strand	14	1	9
α-helix	20-30	11
α-helix	35-39	5
β-strand	44-47	4	8
α-helix	52-54	3
β-strand	62-64	3	8
β-strand	70-72	3	8
α-helix	74-83	10
α-helix	102-104	3
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	134-139	6
α-helix	141-143	3
α-helix	145-148	4
α-helix	152-154	3
α-helix	156-168	13
α-helix	210-243	34
α-helix	250-262	13
α-helix	268-295	28
β-strand	304	1	8
α-helix	316-326	11

Chain D: 4 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	126-127	2	10
β-strand	139-146	8	10
α-helix	147-148	2
β-strand	156-164	9	10
β-strand	168-181	14	10
β-strand	184-197	14	10
β-strand	203-216	14	10
β-strand	237-251	15	10
α-helix	264-269	6
β-strand	273-283	11	10
β-strand	297-306	10	10
β-strand	310-322	13	10
β-strand	330-341	12	10
α-helix	350-352	3
β-strand	357	1	11
β-strand	368	1	12
β-strand	376	1	13
β-strand	381	1	13
β-strand	384	1	11
β-strand	386-395	10	10
β-strand	408-420	13	10
α-helix	428-433	6
β-strand	439-449	11	10
β-strand	454-464	11	10
β-strand	471	1	12
β-strand	474-478	5	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitochondrial outer membrane beta-barrel protein	A, D	protein	363	Saccharomyces cerevisiae	E9P977 (AlphaFold model)
Sorting assembly machinery 35 kDa subunit	B	protein	329	Saccharomyces cerevisiae	P14693 (AlphaFold model)
SAM37 isoform 1	C	protein	327	Saccharomyces cerevisiae	A0A6A5PPM7

Sequence of entity 1 (A, D), FASTA

>7BTW_1 Mitochondrial outer membrane beta-barrel protein (chains A, D)
TFTAKTGTNFGNDNDAEAYLQFEKLIDKKYLKLPTRVNLEILRGTKIHSSFLFNSYSSLS
PQSILNLKVFSQFYNWNTNKGLDIGQRGARLSLRYEPLFLHKLLHNPHSNESPTLFHEWF
LETCWRSTKICSQGTSAPYMYSGTMLSQAGDQLRTILGHTFVLDKRDHIMCPTKGSMLKW
SNELSPGKHLKTQLELNSVKSWMNDDFITFSTTIKTGYLKNLSSQQSLPVHICDKFQSGG
PSDIRGFQTFGLGPRDLYDAVGGDAFVSYGLSVFSRLPWKKVEKSNFRLHWFFNGGKLVN
HDNTSLGNCIGQLSKEHSTSTGIGLVLRHPMARFELNFTLPITAHENDLIRKGFQFGLGL
AFL

Sequence of entity 2 (B), FASTA

>7BTW_2 Sorting assembly machinery 35 kDa subunit (chains B)
MVSSFSVPMPVKRIFDTFPLQTYAAQTDKDEAVALEIQRRSYTFTERGGGSSELTVEGTY
KLGVYNVFLEANTGAALATDPWCLFVQLALCQKNGLVLPTHSQEQTPSHTCNHEMLVLSR
LSNPDEALPILVEGYKKRIIRSTVAISEIMRSRILDDAEQLMYYTLLDTVLYDCWITQII
FCASDAQFMELYSCQKLSGSIVTPLDVENSLLQKLSAKSLKISLTKRNKFQFRHREIVKS
MQGVYHNHHNSVNQEQVLNVLFENSKQVLLGLKDMLKSDGQPTYLHLKIASYILCITNVK
EPIKLKTFVENECKELVQFAQDTLKNFVQ

Sequence of entity 3 (C), FASTA

>7BTW_3 SAM37 isoform 1 (chains C)
MVKGSVHLWGKDGEASLISVDSIALVWFIKLCTSEEAKSMVAGLQIVFSNNTDLSSDGKL
PVLILDNGTKVSGYVNIVQFLHKNICTSKYEKGTDYEEDLAIVGKKDRLLEYSLLNYVDV
EISRLTDYQLFLNTKNYNEYTKKLFSKLLYFPMWYNTPLQLRSQARENCEEIIGSLTLED
DEEFVESKAMESASQLAQSKTFKIAHKNKIKGKQELQQVKYNLQFDNRLQSCVSNWLAAR
KKLDDSVILSSDLLFLANLYVQLGLPDGNRIRSKLEQTFGSELLNSMSNKIDDFVHRPSN
NLEQRDPQFREQGNVVMSLYNLACKYI

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
7BTY 3.2 Å, The mitochondrial SAM-Mdm10 supercomplex in Nanodisc from S.cere

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