8QV0: Tubulin alpha-1 chain

Structure of the native microtubule lattice nucleated from the yeast spindle pole body. Determined by electron microscopy at 6.6 Å resolution. Released 24 Apr 2024.

Method: Electron microscopy
Resolution: 6.6 Å
Organism: Saccharomyces cerevisiae
Chains: 26
Atoms: 88,153
Mol. weight: 1310.68 kDa
Released: 24 Apr 2024

Explore 8QV0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8QV0 contains 608 α-helices and 457 β-strands across 26 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.

Chains A, C, D, E, F, G, H, J, K, L, M and N: 23 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	1
α-helix	11-27	17
β-strand	54-56	3	2
β-strand	62-64	3	2
β-strand	66-70	5	1
α-helix	73-80	8
α-helix	83-86	4
α-helix	90-92	3
β-strand	93-95	3	1
α-helix	104-107	4
α-helix	116-129	14
β-strand	135-141	7	1
α-helix	145-161	17
β-strand	166-173	8	1
α-helix	174-175	2
α-helix	184-198	15
β-strand	201-206	6	1
α-helix	207-216	10
α-helix	225-237	13
β-strand	249	1	3
α-helix	253-259	7
β-strand	270-274	5	3
α-helix	289-297	9
α-helix	299-301	3
α-helix	308-310	3
β-strand	312	1	4
β-strand	316-322	7	3
α-helix	326-338	13
β-strand	343	1	4
α-helix	344-345	2
β-strand	352-357	6	3
α-helix	360-361	2
α-helix	369-371	3
β-strand	374-380	7	3
α-helix	383-385	3
α-helix	386-400	15
α-helix	406-412	7
α-helix	416-438	23

Chains B, Q and R: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	5
α-helix	11-28	18
β-strand	30-31	2	6
β-strand	35-36	2	6
α-helix	42-45	4
α-helix	46-48	3
β-strand	51-53	3	7
α-helix	55-57	3
β-strand	59-61	3	7
β-strand	65-67	3	5
α-helix	71-77	7
α-helix	87-89	3
β-strand	90-92	3	5
α-helix	102-106	5
α-helix	113-126	14
β-strand	130-136	7	5
β-strand	138	1	8
α-helix	142-158	17
β-strand	165-166	2	5
α-helix	168	1
β-strand	169	1	8
α-helix	170-172	3
α-helix	181-195	15
β-strand	198-201	4	5
β-strand	202	1	8
α-helix	204-210	7
α-helix	211-215	5
α-helix	222-241	20
α-helix	250-256	7
β-strand	260	1	9
β-strand	263	1	9
β-strand	265-271	7	5
α-helix	286-293	8
β-strand	299	1	5
β-strand	310-318	9	5
α-helix	323-336	14
β-strand	351-353	3	5
α-helix	357-358	2
β-strand	364-371	8	5
α-helix	374-388	15
α-helix	389-391	3
α-helix	396-399	4
α-helix	405-421	17

Chain I: 23 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	34
α-helix	11-27	17
β-strand	54-56	3	35
β-strand	62-64	3	35
β-strand	66-70	5	34
α-helix	73-80	8
α-helix	83-86	4
α-helix	90-92	3
β-strand	93-95	3	34
α-helix	104-107	4
α-helix	116-129	14
β-strand	135-141	7	34
α-helix	145-161	17
β-strand	166-173	8	34
α-helix	174-175	2
β-strand	181	1	36
α-helix	184-198	15
β-strand	201-206	6	34
α-helix	207-216	10
α-helix	225-237	13
β-strand	249	1	37
α-helix	253-259	7
β-strand	270-274	5	37
α-helix	289-297	9
α-helix	299-301	3
α-helix	308-310	3
β-strand	312	1	38
β-strand	316-322	7	37
α-helix	326-338	13
β-strand	343	1	38
α-helix	344-345	2
β-strand	352-357	6	37
α-helix	360-361	2
α-helix	369-371	3
β-strand	374-380	7	37
α-helix	383-385	3
α-helix	386-400	15
α-helix	406-412	7
α-helix	416-438	23

Chains O, P, S, T, V, W, X, Y and Z: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	59
α-helix	11-24	14
α-helix	25-29	5
β-strand	30-31	2	60
β-strand	35-36	2	60
α-helix	42-45	4
α-helix	46-48	3
β-strand	51-53	3	61
α-helix	55-57	3
β-strand	59-61	3	61
β-strand	65-67	3	59
α-helix	71-77	7
α-helix	87-89	3
β-strand	90-92	3	59
α-helix	102-106	5
α-helix	113-126	14
β-strand	130-136	7	59
β-strand	138	1	62
α-helix	142-158	17
β-strand	165-166	2	59
α-helix	168	1
β-strand	169	1	62
α-helix	170-172	3
α-helix	181-195	15
β-strand	198-201	4	59
β-strand	202	1	62
α-helix	204-210	7
α-helix	211-215	5
α-helix	222-241	20
α-helix	250-256	7
β-strand	260	1	63
β-strand	263	1	63
β-strand	265-271	7	59
α-helix	286-293	8
β-strand	299	1	59
β-strand	310-318	9	59
α-helix	323-336	14
β-strand	351-353	3	59
α-helix	357-358	2
β-strand	364-371	8	59
α-helix	374-388	15
α-helix	389-391	3
α-helix	396-399	4
α-helix	405-421	17

Chain U: 24 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	89
α-helix	11-24	14
α-helix	25-29	5
β-strand	30-31	2	90
β-strand	35-36	2	90
α-helix	42-45	4
α-helix	46-48	3
β-strand	51-53	3	91
α-helix	55-57	3
β-strand	59-61	3	91
β-strand	65-67	3	89
α-helix	71-77	7
α-helix	87-89	3
β-strand	90-92	3	89
α-helix	102-106	5
α-helix	113-126	14
β-strand	130-136	7	89
β-strand	138	1	92
α-helix	142-158	17
β-strand	165-166	2	89
α-helix	168	1
β-strand	169	1	92
α-helix	170-172	3
α-helix	181-195	15
β-strand	198-201	4	89
β-strand	202	1	92
α-helix	204-210	7
α-helix	211-215	5
α-helix	222-241	20
α-helix	250-256	7
β-strand	260	1	93
β-strand	263	1	93
β-strand	265-271	7	89
α-helix	286-293	8
β-strand	299	1	89
β-strand	310-318	9	89
α-helix	323-336	14
β-strand	350	1	36
β-strand	351-353	3	89
α-helix	357-358	2
β-strand	364-371	8	89
α-helix	374-388	15
α-helix	389-391	3
α-helix	396-399	4
α-helix	405-421	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin alpha-1 chain	A, C, D, E, F, G, H, I, J, K, L, M, N	protein	447	Saccharomyces cerevisiae	P09733 (AlphaFold model)
Tubulin beta chain	B, O, P, Q, R, S, T, U, V, W, X, Y, Z	protein	457	Saccharomyces cerevisiae	P02557 (AlphaFold model)

Sequence of entity 1 (A, C, D, E, F, G, H, I, J, K, L, M, N), FASTA

>8QV0_1 Tubulin alpha-1 chain (chains A, C, D, E, F, G, H, I, J, K, L, M, N)
MREVISINVGQAGCQIGNACWELYSLEHGIKPDGHLEDGLSKPKGGEEGFSTFFHETGYG
KFVPRAIYVDLEPNVIDEVRNGPYKDLFHPEQLISGKEDAANNYARGHYTVGREILGDVL
DRIRKLADQCDGLQGFLFTHSLGGGTGSGLGSLLLEELSAEYGKKSKLEFAVYPAPQVST
SVVEPYNTVLTTHTTLEHADCTFMVDNEAIYDMCKRNLDIPRPSFANLNNLIAQVVSSVT
ASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVSYSPVLSKSKAFHESNSVSEITNACFEPG
NQMVKCDPRDGKYMATCLLYRGDVVTRDVQRAVEQVKNKKTVQLVDWCPTGFKIGICYEP
PTATPNSQLATVDRAVCMLSNTTSIAEAWKRIDRKFDLMYAKRAFVHWYVGEGMEEGEFT
EAREDLAALERDYIEVGADSYAEEEEF

Sequence of entity 2 (B, O, P, Q, R, S, T, U, V, W, X, Y, Z), FASTA

>8QV0_2 Tubulin beta chain (chains B, O, P, Q, R, S, T, U, V, W, X, Y, Z)
MREIIHISTGQCGNQIGAAFWETICGEHGLDFNGTYHGHDDIQKERLNVYFNEASSGKWV
PRSINVDLEPGTIDAVRNSAIGNLFRPDNYIFGQSSAGNVWAKGHYTEGAELVDSVMDVI
RREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFPDRMMATFSVLPSPKTSDTVV
EPYNATLSVHQLVEHSDETFCIDNEALYDICQRTLKLNQPSYGDLNNLVSSVMSGVTTSL
RYPGQLNSDLRKLAVNLVPFPRLHFFMVGYAPLTAIGSQSFRSLTVPELTQQMFDAKNMM
AAADPRNGRYLTVAAFFRGKVSVKEVEDEMHKVQSKNSDYFVEWIPNNVQTAVCSVAPQG
LDMAATFIANSTSIQELFKRVGDQFSAMFKRKAFLHWYTSEGMDELEFSEAESNMNDLVS
EYQQYQEATVEDDEEVDENGDFGAPQNQDEPITENFE

Primary citation

Structure of the native gamma-tubulin ring complex capping spindle microtubules. Dendooven, T., Yatskevich, S., Burt, A. et al. Nat Struct Mol Biol (2024) 31:1134-1144. DOI 10.1038/s41594-024-01281-y · PubMed

Other PDB entries of the same protein (UniProt P09733 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4U3J 2.81 Å, TOG2:alpha/beta-tubulin complex
4FFB 2.88 Å, A TOG:alpha/beta-tubulin Complex Structure Reveals Conformation-Based Mechanisms For a…
5W3F 3.7 Å, Yeast tubulin polymerized with GTP in vitro
5W3H 4.0 Å, Yeast microtubule stabilized with epothilone
5W3J 4.0 Å, Yeast microtubule stabilized with Taxol assembled from mutated tubulin
8QV3 8.2 Å, Structure of the y-Tubulin Small Complex (yTuSC) as part of the native y-Tubulin Ring…
8QV2 9.2 Å, Structure of the native y-Tubulin Ring Complex (yTuRC) capping microtubule minus ends at…

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