4U3J: TOG2:alpha/beta-tubulin complex

TOG2:alpha/beta-tubulin complex. Determined by X-ray diffraction at 2.81 Å resolution. Released 20 Aug 2014.

Method: X-ray diffraction
Resolution: 2.81 Å
Organism: Saccharomyces cerevisiae
Chains: 3
Atoms: 8,524
Mol. weight: 131.69 kDa
Ligands: GTP, MG
Released: 20 Aug 2014

Explore 4U3J in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4U3J contains 66 α-helices and 37 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
β-strand	54-56	3	3
β-strand	62-64	3	3
β-strand	66-70	5	1
α-helix	73-81	9
β-strand	93-95	3	1
α-helix	104-105	2
α-helix	106-110	5
α-helix	112-127	16
β-strand	135-141	7	1
α-helix	146-150	5
α-helix	151-161	11
β-strand	166-173	8	1
α-helix	176-178	3
α-helix	184-195	12
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
α-helix	360-361	2
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	406-410	5
α-helix	417-436	20

Chain B: 25 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	6
α-helix	10-27	18
β-strand	30	1	7
β-strand	36	1	7
α-helix	42-45	4
α-helix	46-49	4
β-strand	51-53	3	8
β-strand	59-61	3	8
β-strand	63-67	5	6
α-helix	70-77	8
α-helix	87-89	3
β-strand	90-92	3	6
α-helix	101-105	5
α-helix	113-125	13
β-strand	132-138	7	6
α-helix	143-147	5
α-helix	148-158	11
β-strand	163-170	8	6
α-helix	171	1
α-helix	181-195	15
β-strand	198-203	6	6
α-helix	204-211	8
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	9
α-helix	283-285	3
α-helix	286-294	9
α-helix	296-298	3
β-strand	299	1	9
α-helix	305-307	3
β-strand	310-319	10	9
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	9
β-strand	349-354	6	9
β-strand	363-371	9	9
α-helix	372-374	3
α-helix	375-389	15
α-helix	396-399	4
α-helix	405-426	22

Chain C: 17 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	322	1	10
α-helix	325-327	3
α-helix	332-336	5
α-helix	341-354	14
α-helix	356-358	3
β-strand	362	1	10
α-helix	370-382	13
α-helix	386-403	18
α-helix	410-422	13
α-helix	423-425	3
α-helix	429-445	17
α-helix	456-465	10
α-helix	471-487	17
α-helix	493-497	5
α-helix	499-503	5
α-helix	504-511	8
α-helix	516-533	18
α-helix	539-542	4
α-helix	547-558	12

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	249	Saccharomyces cerevisiae	P46675 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4U3J_1 Tubulin alpha-1 chain (chains A)
MREVISINVGQAGCQIGNACWELYSLEHGIKPDGHLEDGLSKPKGGEEGFSTFFHETGYG
KFVPRAIYVDLEPNVIDEVRNGPYKDLFHPEQLISGKEDAANNYARGHYTVGREILGDVL
DRIRKLADQCDGLQGFLFTHSLGGGTGSGLGSLLLEELSAEYGKKSKLEFAVYPAPQVST
SVVEPYNTVLTTHTTLEHADCTFMVDNEAIYDMCKRNLDIPRPSFANLNNLIAQVVSSVT
ASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVSYSPVLSKSKAFHESNSVSEITNACFEPG
NQMVKCDPRDGKYMATCLLYRGDVVTRDVQRAVEQVKNKKTVQLVDWCPTGFKIGICYEP
PTATPNSQLATVDRAVCMLSNTTSIAEAWKRIDRKFDLMYAKRAFVHWYVGEGMEEGEFT
EAREDLAALERDYIEVGADSYAEEEEF

Sequence of entity 2 (B), FASTA

>4U3J_2 Tubulin beta chain (chains B)
MREIIHISTGQCGNQIGAAFWETICGEHGLDFNGTYHGHDDIQKERLNVYFNEASSGKWV
PRSINVDLEPGTIDAVRNSAIGNLFRPDNYIFGQSSAGNVWAKGHYTEGAELVDSVMDVI
RREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFPDRMMATFSVLPSPKRSDTRV
EPYNATLSVHQLVEHSDETFCIDNEALYDICQRTLKLNQPSYGDLNNLVSSVMSGVTTSL
RYPGQLNSDLRKLAVNLVPFPRLHFFMVGYAPLTAIGSQSFRSLTVPELTQQMFDAKNMM
AAADPRNGRYLTVAAFFRGKVSVKEVEDEMHKVQSKNSDYFVEWIPNNVQTAVCSVAPQG
LDMAATFIANSTSIQELFKRVGDQFSAMFKRKAFLHWYTSEGMDELEFSEAESNMNDLVS
EYQQYQEATVEDDEEVDENGDFGAPQNQDEPITENFEHHHHHH

Sequence of entity 3 (C), FASTA

>4U3J_3 Protein STU2 (chains C)
MLPEETILDKLPKDFQERITSSKWKDRVEALEEFWDSVLSQTKKLKSTSQNYSNLLGIYG
HIIQKDANIQAVALAAQSVELICDKLKTPGFSKDYVSLVFTPLLDRTKEKKPSVIEAIRK
ALLTICKYYDPLASSGRNEDMLKDILEHMKHKTPQIRMECTQLFNASMKEEKDGYSTLQR
YLKDEVVPIVIQIVNDTQPAIRTIGFESFAILIKIFGMNTFVKTLEHLDNLKRKKIEETV
KTLHHHHHH

Ligands and cofactors

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

Primary citation

A tethered delivery mechanism explains the catalytic action of a microtubule polymerase. Ayaz, P., Munyoki, S., Geyer, E.A. et al. Elife (2014) 3:e03069-e03069. DOI 10.7554/eLife.03069 · PubMed

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

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
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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