7M2W: Tubulin gamma chain

Engineered disulfide cross-linked closed conformation of the Yeast gamma-TuRC(SS). Determined by electron microscopy at 3.0 Å resolution. Released 12 May 2021.

Method: Electron microscopy
Resolution: 3.0 Å
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 12
Atoms: 39,366
Mol. weight: 705.38 kDa
Ligands: GTP
Released: 12 May 2021

Explore 7M2W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7M2W contains 231 α-helices and 114 β-strands across 12 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: 20 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	5
α-helix	12-28	17
β-strand	36	1	6
β-strand	54-56	3	7
β-strand	61	1	6
β-strand	62-64	3	7
β-strand	66-69	4	5
α-helix	73-82	10
α-helix	89-91	3
β-strand	92-93	2	5
α-helix	105-114	10
α-helix	116-128	13
β-strand	135-139	5	5
α-helix	145-161	17
β-strand	166-173	8	5
α-helix	180-196	17
β-strand	200-205	6	5
α-helix	206-216	11
α-helix	225-227	3
α-helix	228-243	16
α-helix	252-259	8
β-strand	267-268	2	5
β-strand	269	1	8
β-strand	271	1	9
β-strand	272	1	8
α-helix	291-297	7
β-strand	304	1	9
β-strand	315-323	9	8
α-helix	328-341	14
β-strand	353-357	5	8
α-helix	358-360	3
β-strand	373-380	8	8
α-helix	381-384	4
α-helix	385-397	13
α-helix	398-400	3
α-helix	404-406	3
α-helix	416-440	25
α-helix	444-450	7

Chain B: 19 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	1
α-helix	11-28	18
β-strand	36	1	2
β-strand	54-56	3	3
β-strand	61	1	2
β-strand	62-64	3	3
β-strand	66-69	4	1
α-helix	73-82	10
α-helix	89-91	3
β-strand	92-93	2	1
α-helix	105-114	10
α-helix	116-128	13
β-strand	133-141	9	1
α-helix	145-161	17
β-strand	166-173	8	1
α-helix	180-197	18
β-strand	200-205	6	1
α-helix	206-216	11
α-helix	224-243	20
α-helix	252-259	8
β-strand	267-268	2	1
β-strand	269-273	5	4
α-helix	291-297	7
α-helix	301-303	3
β-strand	304	1	4
β-strand	315-323	9	4
α-helix	328-341	14
β-strand	352-357	6	4
β-strand	373-380	8	4
α-helix	381-385	5
α-helix	388-397	10
α-helix	404-407	4
α-helix	412-414	3
α-helix	416-440	25
α-helix	443-446	4

Chain C: 20 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	10
α-helix	12-28	17
β-strand	36	1	11
β-strand	54-56	3	12
β-strand	61	1	11
β-strand	62-64	3	12
β-strand	66-69	4	10
α-helix	73-82	10
β-strand	93	1	10
α-helix	105-113	9
α-helix	116-128	13
β-strand	133-141	9	10
α-helix	145	1
α-helix	146-150	5
α-helix	151-158	8
β-strand	166-173	8	10
α-helix	174-175	2
α-helix	180-196	17
β-strand	200-205	6	10
α-helix	206-216	11
α-helix	224-243	20
α-helix	252-259	8
β-strand	267-268	2	10
β-strand	269-273	5	13
α-helix	291-297	7
β-strand	304	1	13
β-strand	315-324	10	13
α-helix	328-341	14
α-helix	351	1
β-strand	352-357	6	13
β-strand	372-380	9	13
α-helix	385-397	13
α-helix	412-414	3
α-helix	416-439	24
α-helix	443-445	3
α-helix	447-451	5

Chain D: 19 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	14
β-strand	7-10	4	15
α-helix	12-27	16
β-strand	36	1	16
β-strand	54-57	4	16
β-strand	61-64	4	16
β-strand	66-69	4	15
α-helix	73-82	10
β-strand	93	1	15
α-helix	105-114	10
α-helix	116-128	13
β-strand	133-136	4	14
β-strand	138-139	2	15
α-helix	145-160	16
β-strand	166	1	14
β-strand	168-173	6	15
α-helix	180-196	17
β-strand	200-205	6	15
α-helix	206-216	11
α-helix	224-226	3
α-helix	228-243	16
α-helix	252-259	8
β-strand	267-268	2	15
β-strand	269	1	17
β-strand	271	1	18
β-strand	272	1	17
α-helix	291-297	7
β-strand	304	1	18
β-strand	315-324	10	17
α-helix	328-339	12
β-strand	353-357	5	17
α-helix	358-360	3
α-helix	368-370	3
β-strand	372-380	9	17
α-helix	381-384	4
α-helix	385-398	14
α-helix	416-440	25
α-helix	443-445	3
α-helix	447-450	4

Chain E: 41 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	19
β-strand	8	1	20
β-strand	12	1	21
β-strand	26	1	21
α-helix	28-31	4
β-strand	39	1	19
α-helix	43-46	4
α-helix	52-66	15
β-strand	75-77	3	22
β-strand	92-94	3	22
α-helix	100-126	27
α-helix	129-131	3
α-helix	132-145	14
α-helix	146-150	5
α-helix	151-153	3
α-helix	154-159	6
α-helix	160-164	5
α-helix	170-179	10
α-helix	182-205	24
α-helix	223-225	3
β-strand	232-235	4	23
α-helix	245-257	13
α-helix	262-275	14
α-helix	277-289	13
β-strand	301-302	2	23
β-strand	324-327	4	23
α-helix	338-360	23
α-helix	381-386	6
α-helix	389-407	19
α-helix	408-412	5
α-helix	415-426	12
α-helix	432-451	20
α-helix	459-470	12
α-helix	477-480	4
β-strand	482-486	5	24
α-helix	491-495	5
β-strand	560-564	5	24
α-helix	566-567	2
α-helix	570-572	3
α-helix	576-608	33
α-helix	610-613	4
α-helix	617-619	3
α-helix	621	1
α-helix	622-627	6
α-helix	628-647	20
α-helix	648-652	5
α-helix	653-662	10
α-helix	669-684	16
α-helix	693-716	24
α-helix	717-720	4
α-helix	722-725	4
α-helix	755-787	33
α-helix	802-811	10

Chain F: 29 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	167-171	5
α-helix	172-175	4
α-helix	181-191	11
β-strand	209	1	20
α-helix	215-241	27
α-helix	248-274	27
α-helix	280-286	7
α-helix	288-300	13
α-helix	304-306	3
α-helix	309-319	11
α-helix	325-352	28
β-strand	364-366	3	25
β-strand	383-385	3	25
α-helix	396-414	19
α-helix	419-434	16
α-helix	437-439	3
α-helix	443-466	24
α-helix	470-480	11
α-helix	486-500	15
α-helix	512-521	10
α-helix	526-529	4
α-helix	535-539	5
β-strand	541-545	5	26
β-strand	558-562	5	26
α-helix	568-570	3
α-helix	582-615	34
α-helix	624-655	32
α-helix	657-668	12
β-strand	681-683	3	27
β-strand	689-691	3	27
α-helix	721-736	16
α-helix	748-749	2
β-strand	750	1	28
α-helix	751	1
β-strand	757	1	28
α-helix	758-792	35
α-helix	800-831	32
α-helix	836-844	9

Chain G: 43 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	29
β-strand	8	1	30
β-strand	12	1	31
β-strand	26	1	31
α-helix	27-31	5
β-strand	38	1	29
α-helix	43-46	4
α-helix	52-66	15
β-strand	75-77	3	32
β-strand	92-94	3	32
α-helix	100-126	27
α-helix	132-145	14
α-helix	146-150	5
α-helix	151-153	3
α-helix	154-159	6
α-helix	160-164	5
α-helix	170-179	10
α-helix	182-205	24
α-helix	224-227	4
β-strand	232-235	4	33
α-helix	245-257	13
α-helix	262-275	14
α-helix	277-288	12
β-strand	301-303	3	33
β-strand	324-327	4	33
α-helix	328-330	3
α-helix	338-360	23
α-helix	381-384	4
α-helix	389-407	19
α-helix	408-413	6
α-helix	415-422	8
α-helix	423-427	5
α-helix	432-441	10
α-helix	445-447	3
α-helix	459-470	12
α-helix	477-481	5
β-strand	483-486	4	34
α-helix	491-495	5
α-helix	556-558	3
β-strand	560-563	4	34
α-helix	566-567	2
α-helix	576-608	33
α-helix	610-613	4
α-helix	617-619	3
α-helix	621	1
α-helix	622-627	6
α-helix	628-647	20
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	722-724	3
α-helix	755-788	34
α-helix	803-811	9

Chain H: 30 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	167-171	5
α-helix	172-174	3
α-helix	181-191	11
β-strand	209	1	30
α-helix	215-241	27
α-helix	248-274	27
α-helix	280-286	7
α-helix	288-300	13
α-helix	304-306	3
α-helix	309-319	11
α-helix	325-352	28
β-strand	364-366	3	35
β-strand	383-385	3	35
α-helix	387-389	3
α-helix	396-414	19
α-helix	419-434	16
α-helix	443-468	26
α-helix	470-478	9
α-helix	486-495	10
α-helix	497-500	4
α-helix	511-521	11
α-helix	526-529	4
α-helix	535-538	4
β-strand	541-545	5	36
α-helix	554-557	4
β-strand	558-562	5	36
α-helix	568-571	4
α-helix	582-612	31
α-helix	622-655	34
α-helix	657-668	12
β-strand	681-683	3	37
β-strand	689-691	3	37
α-helix	721-737	17
α-helix	748-750	3
β-strand	751	1	38
β-strand	756	1	38
α-helix	758-792	35
α-helix	801-831	31
α-helix	836-845	10

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin gamma chain	A, B, C, D	protein	473	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P53378 (AlphaFold model)
Spindle pole body component SPC97	E, G	protein	823	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P38863 (AlphaFold model)
Spindle pole body component SPC98	F, H	protein	846	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P53540 (AlphaFold model)
Spindle pole body component 110	K, U, X, Y	protein	220	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P32380 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>7M2W_1 Tubulin gamma chain (chains A, B, C, D)
MGGEIITLQAGQCGNHVGKFLWSQLAKEHAIGTDGLSQLPDSSTERDDDTKPFFRENCRN
KFTPRAIMMDSEPSVIADVENTFRGFFDPRNTWVASDGASAGNSWANGYDIGTRNQDDIL
NKIDKEIDSTDNFEGFQLLHSVAGGTGSGLGSNLLEALCDRYPKKILTTYSVFPARSSEV
VVQSYNTILALRRLIEDSDATVVFDNASLLNISGKVFRNPNIDLQHTNQLISTIISSVTN
SIRFPSYMYSSMSSIYSTLIPSPELHFLSPSFTPFTSDYIHDDIAHKCHSSYDVMLDLLD
PSNSLVSTAMNNPTYFNVYNTIIGNVEPRQISRAMTKLQQRIKFPSWSSSAMHVNIGRRS
PYLPLQPNENEVSGMMLSNMSTVVNVFENACNTFDKVFAKGAFLNNYNVGDLFQSMQNVQ
DEFAESREVVQSLMEDYVAAEQDSYLDDVLVDDENMVGELEEDLDADGDHKLV

Sequence of entity 2 (E, G), FASTA

>7M2W_2 Spindle pole body component SPC97 (chains E, G)
MEIKEVDDRAELLRYTNNIPLLGKLVNHQPLWSTNPKLKSFSLEKISAPDQRRVQEALVV
KDLLNVLIGLEGTYIRYFNDYEPSDPETPIEFKIAKKMDPSFKTFSRRIVRYGKQYMILT
RAYEKWSDTSFGMVLQRFAYEIRRFLEDVYLKTLVERLERDFNKVPNFSIRELEQIINET
EVNKQMELLYNIYEEIFREIEERRTNQSSQEDFNNFMDSMKNESSLHLRLMVAFDTTVYP
VPKGGAILKIFQQKILENLGDRSSVMFLKKLLNNISQDYCTMLYEWLTQGILNDPYQEFM
TYDDLEGKTDNIFDTRDRAWDTQYFIRKDVLLRDCDSEEDKNLLFKMLRTGILLKVVRAS
LQIPTIPSNSSDITIQEINDFADLMEGSNLELYVDKCYSRANEIFLKLFFQGYDLINVLK
HLQQIFLGYQSGHNVLKFLTKNMGELTKHYRNDNNANYDKLLQNFELERQSENPNNLMRQ
LLMIQFDTETLPQVLSHYLQIYPEVPENNSANDDSDPLMHANNFKNMNAILFDELSKERT
GAYHGSNLELYTPKSAIYHLKFDINIPYPLNIIISRTCMIKYQIILRYQLVLQYHSRLLD
ETWMDLNKTPSWKYRGYSHTVKRRIVRATRVLHAKMNHFIKTIMEYFNQNVIDKEVYSLE
KCYRNPTLAVAIQNELEGGLTNIMTNRCLSDLIPLQLQIFDIVYKFCKFIKSMRAKLCQL
DPVLYEKHKSGMMKTLNEGYRTNNGGQEDVGYQEDAALELIQKLIEYISNASSIFRKCLI
NFTQELSTEKFDFYDSSSVDAAGIERVLYSIVPPRSASASSQR

Sequence of entity 3 (F, H), FASTA

>7M2W_3 Spindle pole body component SPC98 (chains F, H)
MELEPTLFGIIEALAPQLLSQSHLQTFVSDVVNLLRSSTKSATQLGPLIDFYKLQSLDSP
ETTIMWHKIEKFLDALFGIQNTDDMVKYLSVFQSLLPSNYRAKIVQKSSGLNMENLANHE
HLLSPVRAPSIYTEASFENMDRFSERRSMVSSPNRYVPSSTYSSVTLRQLSNPYYVNTIP
EEDILKYVSYTLLATTSALFPFDHEQIQIPSKIPNFESGLLHLIFEAGLLYQSLGYKVEK
FRMLNISPMKKALIIEISEELQNYTAFVNNLVSSGTVVSLKSLYREIYENIIRLRIYCRF
TEHLEELSGDTFLIELNIFKSHGDLTIRKIATNLFNSMISLYYEYLMNWLTKGLLRATYG
EFFIAENTDTNGTDDDFIYHIPIEFNQERVPAFIPKELAYKIFMIGKSYIFLEKYCKEVQ
WTNEFSKKYHVLYQSNSYRGISTNFFEIINDQYSEIVNHTNQILNQKFHYRDVVFALKNI
LLMGKSDFMDALIEKANDILATPSDSLPNYKLTRVLQEAVQLSSLRHLMNSPRNSSVING
LDARVLDLGHGSVGWDVFTLDYILYPPLSLVLNVNRPFGRKEYLRIFNFLWRFKKNNYFY
QKEMLKSNDIIRSFKKIRGYNPLIRDIINKLSRISILRTQFQQFNSKMESYYLNCIIEEN
FKEMTRKLQRTENKSQNQFDLIRLNNGTIELNGILTPKAEVLTKSSSSKPQKHAIEKTLN
IDELESVHNTFLTNILSHKLFATNTSEISVGDYSGQPYPTSLVLLLNSVYEFVKVYCNLN
DIGYEIFIKMNLNDHEASNGLLGKFNTNLKEIVSQYKNFKDRLYIFRADLKNDGDEELFL
LSKSLR

Sequence of entity 4 (K, U, X, Y), FASTA

>7M2W_4 Spindle pole body component 110 (chains K, U, X, Y)
MDEASHLPNGSLKNMEFTPVGFIKSKRNTTQTQVVSPTKVPNANNGDENEGPVKKRQRRS
IDDTIDSTRLFSEASQFDDSFPEIKANIPPSPRSGNVDKSRKRNLIDDLKKDVPMSQPLK
EQEVREHQMKKERFDRALESKLLGKRHITYANSDISNKELYINEIKSLKHEIKELRKEKN
DTLNNYDTLEEETDDLKNRLQALEKELDAKNKIVNSRKVD

Ligands and cofactors

ID	Name	Formula	Copies
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	4

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:

7M2X 3.6 Å, Open conformation of the Yeast wild-type gamma-TuRC
7M2Z 3.7 Å, Monomeric single-particle reconstruction of the Yeast gamma-TuSC
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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