4FFB: Tubulin alpha-1 chain

A TOG:alpha/beta-tubulin Complex Structure Reveals Conformation-Based Mechanisms For a Microtubule Polymerase. Determined by X-ray diffraction at 2.88 Å resolution. Released 15 Aug 2012.

Method: X-ray diffraction
Resolution: 2.88 Å
Organism: Saccharomyces cerevisiae
Chains: 3
Atoms: 8,535
Mol. weight: 134.53 kDa
Ligands: MG, GTP
Released: 15 Aug 2012

Explore 4FFB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4FFB contains 62 α-helices and 33 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: 24 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	1
α-helix	10-27	18
β-strand	30	1	2
β-strand	36	1	2
α-helix	37	1
α-helix	50-53	4
β-strand	54-58	5	3
β-strand	61-64	4	3
β-strand	66-70	5	1
α-helix	74-80	7
α-helix	90-92	3
β-strand	93-95	3	1
α-helix	104-108	5
α-helix	112-114	3
α-helix	116-128	13
β-strand	135-141	7	1
α-helix	146-161	16
β-strand	166-173	8	1
α-helix	176-178	3
α-helix	184-194	11
β-strand	201-206	6	1
α-helix	207-216	10
α-helix	225-239	15
α-helix	241-244	4
α-helix	253-260	8
α-helix	269	1
β-strand	270-274	5	4
β-strand	278	1	5
α-helix	289-295	7
α-helix	299-301	3
β-strand	302	1	4
β-strand	313-322	10	4
α-helix	326-338	13
β-strand	344	1	4
β-strand	352-357	6	4
β-strand	369	1	5
α-helix	370-371	2
β-strand	374-382	9	4
α-helix	383-385	3
α-helix	386-400	15
α-helix	407-410	4
α-helix	417-435	19

Chain B: 23 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	6
α-helix	10-28	19
α-helix	42-45	4
α-helix	46-48	3
β-strand	51-54	4	7
β-strand	58-61	4	7
β-strand	63-67	5	6
α-helix	70-77	8
α-helix	80-82	3
α-helix	87-89	3
β-strand	90-92	3	6
α-helix	101-105	5
α-helix	110-124	15
β-strand	132-138	7	6
α-helix	143-147	5
α-helix	148-158	11
β-strand	163-170	8	6
α-helix	181-195	15
β-strand	198-203	6	6
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-236	15
α-helix	238-241	4
α-helix	250-257	8
β-strand	265-266	2	6
β-strand	267-271	5	8
α-helix	286-294	9
α-helix	296-298	3
β-strand	299	1	8
β-strand	310-319	10	8
α-helix	323-336	14
β-strand	341	1	8
β-strand	349-354	6	8
β-strand	363-371	9	8
α-helix	372-374	3
α-helix	375-389	15
α-helix	395-399	5
α-helix	405-424	20

Chain C: 15 helices, 0 β-strands

Element	Residues	Length
α-helix	14-17	4
α-helix	23-38	16
α-helix	58-63	6
α-helix	69-83	15
α-helix	93-110	18
α-helix	117-132	16
α-helix	138-144	7
α-helix	145-149	5
α-helix	153-170	18
α-helix	177-184	8
α-helix	185-187	3
α-helix	188-192	5
α-helix	197-211	15
α-helix	231-241	11
α-helix	256-268	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin alpha-1 chain	A	protein	447	Saccharomyces cerevisiae	P09733 (AlphaFold model)
Tubulin beta chain	B	protein	463	Saccharomyces cerevisiae	P02557 (AlphaFold model)
Protein STU2	C	protein	278	Saccharomyces cerevisiae	P46675 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4FFB_1 Tubulin alpha-1 chain (chains A)
MREVISINVGQAGCQIGNACWELYSLEHGIKPDGHLEDGLSKPKGGEEGFSTFFHETGYG
KFVPRAIYVDLEPNVIDEVRNGPYKDLFHPEQLISGKEDAANNYARGHYTVGREILGDVL
DRIRKLADQCDGLQGFLFTHSLGGGTGSGLGSLLLEELSAEYGKKSKLEFAVYPAPQVST
SVVEPYNTVLTTHTTLEHADCTFMVDNEAIYDMCKRNLDIPRPSFANLNNLIAQVVSSVT
ASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVSYSPVLSKSKAFHESNSVSEITNACFEPG
NQMVKCDPRDGKYMATCLLYRGDVVTRDVQRAVEQVKNKKTVQLVDWCPTGFKIGICYEP
PTATPNSQLATVDRAVCMLSNTTSIAEAWKRIDRKFDLMYAKRAFVHWYVGEGMEEGEFT
EAREDLAALERDYIEVGADSYAEEEEF

Sequence of entity 2 (B), FASTA

>4FFB_2 Tubulin beta chain (chains B)
MREIIHISTGQCGNQIGAAFWETICGEHGLDFNGTYHGHDDIQKERLNVYFNEASSGKWV
PRSINVDLEPGTIDAVRNSAIGNLFRPDNYIFGQSSAGNVWAKGHYTEGAELVDSVMDVI
RREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFPDRMMATFSVLPSPKRSDTRV
EPYNATLSVHQLVEHSDETFCIDNEALYDICQRTLKLNQPSYGDLNNLVSSVMSGVTTSL
RYPGQLNSDLRKLAVNLVPFPRLHFFMVGYAPLTAIGSQSFRSLTVPELTQQMFDAKNMM
AAADPRNGRYLTVAAFFRGKVSVKEVEDEMHKVQSKNSDYFVEWIPNNVQTAVCSVAPQG
LDMAATFIANSTSIQELFKRVGDQFSAMFKRKAFLHWYTSEGMDELEFSEAESNMNDLVS
EYQQYQEATVEDDEEVDENGDFGAPQNQDEPITENFEHHHHHH

Sequence of entity 3 (C), FASTA

>4FFB_3 Protein STU2 (chains C)
MSGEEEVDYTTLPLEERLTYKLWKARLEAYKELNQLFRNSVGDISRDDNIQIYWRDPTLF
AQYITDSNVVAQEQAIVALNSLIDAFASSSLKNAHNITLISTWTPLLVEKGLTSSRATTK
TQSMSCILSLCGLDTSITQSVELVIPFFEKKLPKLIAAAANCVYELMAAFGLTNVNVQTF
LPELLKHVPQLAGHGDRNVRSQTMNLIVEIYKVTGNNSDLLEEILFKKLKPIQVKDLHKL
FAKVGDEPSSSKMLFEWEKRELEKKRSQEEEAHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	2

Primary citation

A TOG: alpha beta-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase. Ayaz, P., Ye, X., Huddleston, P. et al. Science (2012) 337:857-860. DOI 10.1126/science.1221698 · 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
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
8QV0 6.6 Å, Structure of the native microtubule lattice nucleated from the yeast spindle pole body
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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