7M2Z: Tubulin gamma chain

Monomeric single-particle reconstruction of the Yeast gamma-TuSC. Determined by electron microscopy at 3.7 Å resolution. Released 12 May 2021.

Method: Electron microscopy
Resolution: 3.7 Å
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 4
Atoms: 18,330
Mol. weight: 301.51 kDa
Ligands: GDP
Released: 12 May 2021

Explore 7M2Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7M2Z contains 101 α-helices and 50 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: 17 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	6
α-helix	11-28	18
β-strand	54-56	3	7
β-strand	62-64	3	7
β-strand	66-69	4	6
α-helix	74-80	7
α-helix	89-91	3
β-strand	93	1	6
α-helix	100	1
α-helix	105-127	23
β-strand	133-139	7	6
α-helix	145-161	17
β-strand	166-173	8	6
α-helix	179-181	3
α-helix	183-197	15
β-strand	200-205	6	6
α-helix	206-216	11
α-helix	224-243	20
α-helix	252-256	5
β-strand	267-272	6	6
α-helix	291-297	7
α-helix	301-303	3
β-strand	304	1	6
β-strand	315-324	10	6
α-helix	328-341	14
β-strand	352-354	3	6
β-strand	372-380	9	6
α-helix	384-397	14
α-helix	405-407	3
α-helix	416-441	26

Chain B: 16 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	1
β-strand	8-9	2	2
α-helix	12-28	17
β-strand	31	1	3
β-strand	37	1	3
β-strand	55-56	2	4
β-strand	62-63	2	4
β-strand	67-69	3	2
α-helix	73-82	10
α-helix	89-91	3
β-strand	92-93	2	2
α-helix	104-127	24
β-strand	133-136	4	1
β-strand	139-141	3	2
α-helix	145-158	14
β-strand	166-167	2	1
β-strand	168-173	6	2
α-helix	183-194	12
β-strand	200-205	6	2
α-helix	206-216	11
α-helix	229-237	9
α-helix	252-259	8
β-strand	267-268	2	2
β-strand	269-271	3	5
α-helix	291-297	7
β-strand	315-323	9	5
α-helix	328-341	14
β-strand	353-356	4	5
β-strand	373-380	8	5
α-helix	381-384	4
α-helix	385-391	7
α-helix	394-398	5
α-helix	416-441	26
α-helix	447-450	4

Chain C: 28 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	167-171	5
α-helix	181-191	11
β-strand	197	1	8
β-strand	200	1	8
β-strand	207-209	3	9
α-helix	215-241	27
α-helix	248-274	27
α-helix	280-300	21
α-helix	309-319	11
α-helix	325-352	28
β-strand	364-366	3	10
β-strand	383-385	3	10
α-helix	387-389	3
α-helix	396-411	16
α-helix	412-416	5
α-helix	419-434	16
α-helix	443-466	24
α-helix	473-480	8
α-helix	486-495	10
α-helix	497-500	4
α-helix	509-522	14
α-helix	526-530	5
α-helix	536-539	4
β-strand	541-544	4	11
β-strand	559-562	4	11
α-helix	568-571	4
α-helix	582-614	33
α-helix	622-651	30
α-helix	652-656	5
α-helix	657-669	13
β-strand	681-683	3	12
β-strand	689-691	3	12
α-helix	721-736	16
α-helix	750-751	2
α-helix	758-791	34
α-helix	800-833	34
α-helix	836-844	9

Chain D: 40 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	9
β-strand	12	1	13
β-strand	26	1	13
α-helix	27-29	3
α-helix	43-46	4
α-helix	49-51	3
α-helix	52-66	15
β-strand	75-77	3	14
β-strand	92-94	3	14
α-helix	100-103	4
α-helix	106-125	20
α-helix	129-131	3
α-helix	133-144	12
α-helix	145-155	11
α-helix	156-164	9
α-helix	170-179	10
α-helix	182-205	24
β-strand	232-234	3	15
α-helix	244-257	14
α-helix	262-275	14
α-helix	277-289	13
β-strand	301-302	2	15
β-strand	324-326	3	15
α-helix	328-330	3
α-helix	338-361	24
α-helix	368-370	3
α-helix	381-386	6
α-helix	390-407	18
α-helix	408-412	5
α-helix	415-426	12
α-helix	432-449	18
α-helix	459-471	13
α-helix	477-480	4
β-strand	483-486	4	16
α-helix	491-495	5
β-strand	560-563	4	16
α-helix	571-573	3
α-helix	577-606	30
α-helix	610-612	3
α-helix	619-621	3
α-helix	622-626	5
α-helix	627-647	21
α-helix	648-652	5
α-helix	653-662	10
α-helix	669-684	16
α-helix	687-690	4
α-helix	693-716	24
α-helix	717-719	3
α-helix	758-788	31
α-helix	808-810	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin gamma chain	A, B	protein	473	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P53378 (AlphaFold model)
Spindle pole body component SPC98	C	protein	846	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P53540 (AlphaFold model)
Spindle pole body component SPC97	D	protein	823	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P38863 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7M2Z_1 Tubulin gamma chain (chains A, B)
MGGEIITLQAGQCGNHVGKFLWSQLAKEHAIGTDGLSQLPDSSTERDDDTKPFFRENSRN
KFTPRAIMMDSEPSVIADVENTFRGFFDPRNTWVASDGASAGNSWANGYDIGTRNQDDIL
NKIDKEIDSTDNFEGFQLLHSVAGGTGSGLGSNLLEALCDRYPKKILTTYSVFPARSSEV
VVQSYNTILALRRLIEDSDATVVFDNASLLNISGKVFRNPNIDLQHTNQLISTIISSVTN
SIRFPSYMYSSMSSIYSTLIPSPELHFLSPSFTPFTSDYIHDDIAHKGHSSYDVMLDLLD
PSNSLVSTAMNNPTYFNVYNTIIGNVEPRQISRAMTKLQQRIKFPSWSSSAMHVNIGRRS
PYLPLQPNENEVSGMMLSNMSTVVNVFENACNTFDKVFAKGAFLNNYNVGDLFQSMQNVQ
DEFAESREVVQSLMEDYVAAEQDSYLDDVLVDDENMVGELEEDLDADGDHKLV

Sequence of entity 2 (C), FASTA

>7M2Z_2 Spindle pole body component SPC98 (chains C)
MELEPTLFGIIEALAPQLLSQSHLQTFVSDVVNLLRSSTKSATQLGPLIDFYKLQSLDSP
ETTIMWHKIEKFLDALFGIQNTDDMVKYLSVFQSLLPSNYRAKIVQKSSGLNMENLANHE
HLLSPVRAPSIYTEASFENMDRFSERRSMVSSPNRYVPSSTYSSVTLRQLSNPYYVNTIP
EEDILKYVSYTLLATTSALFPFDHEQIQIPSKIPNFESGLLHLIFEAGLLYQSLGYKVEK
FRMLNISPMKKALIIEISEELQNYTAFVNNLVSSGTVVSLKSLYREIYENIIRLRIYCRF
TEHLEELSGDTFLIELNIFKSHGDLTIRKIATNLFNSMISLYYEYLMNWLTKGLLRATYG
EFFIAENTDTNGTDDDFIYHIPIEFNQERVPAFIPKELAYKIFMIGKSYIFLEKYCKEVQ
WTNEFSKKYHVLYQSNSYRGISTNFFEIINDQYSEIVNHTNQILNQKFHYRDVVFALKNI
LLMGKSDFMDALIEKANDILATPSDSLPNYKLTRVLQEAVQLSSLRHLMNSPRNSSVING
LDARVLDLGHGSVGWDVFTLDYILYPPLSLVLNVNRPFGRKEYLRIFNFLWRFKKNNYFY
QKEMLKSNDIIRSFKKIRGYNPLIRDIINKLSRISILRTQFQQFNSKMESYYLNCIIEEN
FKEMTRKLQRTENKSQNQFDLIRLNNGTIELNGILTPKAEVLTKSSSSKPQKHAIEKTLN
IDELESVHNTFLTNILSHKLFATNTSEISVGDYSGQPYPTSLVLLLNSVYEFVKVYCNLN
DIGYEIFIKMNLNDHEASNGLLGKFNTNLKEIVSQYKNFKDRLYIFRADLKNDGDEELFL
LSKSLR

Sequence of entity 3 (D), FASTA

>7M2Z_3 Spindle pole body component SPC97 (chains D)
MEIKEVDDRAELLRYTNNIPLLGKLVNHQPLWSTNPKLKSFSLEKISAPDQRRVQEALVV
KDLLNVLIGLEGTYIRYFNDYEPSDPETPIEFKIAKKMDPSFKTFSRRIVRYGKQYMILT
RAYEKWSDTSFGMVLQRFAYEIRRFLEDVYLKTLVERLERDFNKVPNFSIRELEQIINET
EVNKQMELLYNIYEEIFREIEERRTNQSSQEDFNNFMDSMKNESSLHLRLMVAFDTTVYP
VPKGGAILKIFQQKILENLGDRSSVMFLKKLLNNISQDYCTMLYEWLTQGILNDPYQEFM
TYDDLEGKTDNIFDTRDRAWDTQYFIRKDVLLRDCDSEEDKNLLFKMLRTGILLKVVRAS
LQIPTIPSNSSDITIQEINDFADLMEGSNLELYVDKCYSRANEIFLKLFFQGYDLINVLK
HLQQIFLGYQSGHNVLKFLTKNMGELTKHYRNDNNANYDKLLQNFELERQSENPNNLMRQ
LLMIQFDTETLPQVLSHYLQIYPEVPENNSANDDSDPLMHANNFKNMNAILFDELSKERT
GAYHGSNLELYTPKSAIYHLKFDINIPYPLNIIISRTCMIKYQIILRYQLVLQYHSRLLD
ETWMDLNKTPSWKYRGYSHTVKRRIVRATRVLHAKMNHFIKTIMEYFNQNVIDKEVYSLE
KCYRNPTLAVAIQNELEGGLTNIMTNRCLSDLIPLQLQIFDIVYKFCKFIKSMRAKLCQL
DPVLYEKHKSGMMKTLNEGYRTNNGGQEDVGYQEDAALELIQKLIEYISNASSIFRKCLI
NFTQELSTEKFDFYDSSSVDAAGIERVLYSIVPPRSASASSQR

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2

Primary citation

CM1-driven assembly and activation of yeast gamma-tubulin small complex underlies microtubule nucleation. Brilot, A.F., Lyon, A.S., Zelter, A. et al. Elife (2021) 10. DOI 10.7554/eLife.65168 · PubMed

Other PDB entries of the same protein (UniProt P53378 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7M2W 3.0 Å, Engineered disulfide cross-linked closed conformation of the Yeast gamma-TuRC(SS)
7M2X 3.6 Å, Open conformation of the Yeast wild-type gamma-TuRC
7M2Y 4.03 Å, Closed conformation of the Yeast wild-type gamma-TuRC
5FLZ 6.9 Å, Cryo-EM structure of gamma-TuSC oligomers in a closed conformation
5FM1 8.0 Å, Structure of gamma-tubulin small complex based on a cryo-EM map, chemical cross-links,…
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…
9A15 Integrative structure of the yeast gammaTuSC-Spc110 monomer complex
9A16 Integrative structure of the yeast gammaTuSC-Spc110 dimer complex
9A17 Integrative structure of the yeast gammaTuSC-Spc110 tetramer complex

Browse structure collections

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