8SH7: Tubulin alpha-1A chain

TUBB4B and TUBA1A Heterodimer from Human Respiratory Doublet Microtubules. Determined by electron microscopy at 2.8 Å resolution. Released 1 May 2024.

Method: Electron microscopy
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,819
Mol. weight: 101.06 kDa
Ligands: GDP, MG, GTP
Released: 1 May 2024

Explore 8SH7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8SH7 contains 54 α-helices and 36 β-strands across 2 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: 28 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	1
α-helix	10-28	19
β-strand	35	1	2
α-helix	48-51	4
β-strand	53-55	3	3
β-strand	60	1	2
β-strand	61-63	3	3
β-strand	65-69	5	1
α-helix	72-78	7
α-helix	89-91	3
β-strand	92-94	3	1
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-128	18
β-strand	134-140	7	1
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-171	7	1
α-helix	172-174	3
α-helix	183-196	14
β-strand	200-204	5	1
α-helix	206-215	10
α-helix	224-238	15
α-helix	240-243	4
β-strand	248	1	4
α-helix	252-257	6
α-helix	268	1
β-strand	269-273	5	4
β-strand	277	1	5
α-helix	278-281	4
α-helix	288-295	8
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-321	10	4
α-helix	325-337	13
β-strand	343	1	4
β-strand	351-356	6	4
α-helix	359-361	3
β-strand	368	1	5
α-helix	369-370	2
β-strand	373-381	9	4
α-helix	382-384	3
α-helix	385-399	15
α-helix	405-409	5
α-helix	416-435	20

Chain B: 26 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	6
α-helix	10-28	19
β-strand	30	1	7
β-strand	35	1	8
β-strand	36	1	7
α-helix	41-43	3
α-helix	47-49	3
β-strand	51-54	4	8
β-strand	58-61	4	8
β-strand	63-67	5	6
α-helix	71-77	7
α-helix	81-83	3
α-helix	87-89	3
β-strand	90-92	3	6
α-helix	101-102	2
α-helix	103-107	5
α-helix	109-124	16
β-strand	130-138	9	6
α-helix	143-147	5
α-helix	148-158	11
β-strand	163-169	7	6
α-helix	181-195	15
β-strand	198-202	5	6
α-helix	204-213	10
α-helix	222-241	20
β-strand	244-246	3	9
α-helix	250-257	8
β-strand	265-266	2	6
β-strand	267-271	5	9
α-helix	278-281	4
α-helix	286-294	9
α-helix	296-298	3
α-helix	305-307	3
β-strand	310-318	9	9
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	9
β-strand	349-354	6	9
α-helix	357-358	2
β-strand	364-371	8	9
α-helix	372-374	3
α-helix	375-389	15
α-helix	395-399	5
α-helix	406-423	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin alpha-1A chain	A	protein	451	Homo sapiens	Q71U36 (AlphaFold model)
Tubulin beta-4B chain	B	protein	445	Homo sapiens	P68371 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8SH7_1 Tubulin alpha-1A chain (chains A)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 2 (B), FASTA

>8SH7_2 Tubulin beta-4B chain (chains B)
MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGKYV
PRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEGEFEEEAEEEVA

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
MG	Magnesium ion	Mg	1
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	1

Primary citation

Ciliopathy patient variants reveal organelle-specific functions for TUBB4B in axonemal microtubules. Dodd, D.O., Mechaussier, S., Yeyati, P.L. et al. Science (2024) 384:eadf5489-eadf5489. DOI 10.1126/science.adf5489 · PubMed

Other PDB entries of the same protein (UniProt Q71U36 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9WD9 2.26 Å, GMPCPP-stabilized human alpha1A/beta3 S239C microtubule
6J8F 2.28 Å, Crystal structure of SVBP-VASH1 with peptide mimic the C-terminal of alpha-tubulin
9WD7 2.34 Å, GMPCPP-stabilizsd human alpha1A/beta3 microtubule
9WDA 2.35 Å, Paclitaxel/GMPCPP-stabilized human alpha1A/beta3 microtubule
9WDB 2.39 Å, Paclitaxel/GMPCPP-stabilized human alpha1A/beta3 S239C microtubule
22AK 2.41 Å, GDP human alpha1A/beta3 microtubule
22AJ 2.48 Å, GDP human alpha1A/beta3 S239C microtubule
9OX7 2.69 Å, In situ microtubule structure in the axon of a human neuron
6WSL 3.1 Å, Cryo-EM structure of VASH1-SVBP bound to microtubules
7UNG 3.6 Å, 48-nm repeat of the human respiratory doublet microtubule
5JCO 4.0 Å, Structure and dynamics of single-isoform recombinant neuronal human tubulin
8J07 4.1 Å, 96nm repeat of human respiratory doublet microtubule and associated axonemal complexes

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