7M2Y: Tubulin gamma chain
Closed conformation of the Yeast wild-type gamma-TuRC. Determined by electron microscopy at 4.03 Å resolution. Released 12 May 2021.
- Method
- Electron microscopy
- Resolution
- 4.03 Å
- Organism
- Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
- Chains
- 5
- Atoms
- 18,560
- Mol. weight
- 326.96 kDa
- Ligands
- GDP
- Released
- 12 May 2021
Explore 7M2Y in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7M2Y contains 131 α-helices and 61 β-strands across 5 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: 25 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4 | 1 | 1 |
| β-strand | 7-9 | 3 | 2 |
| α-helix | 11-28 | 18 | |
| β-strand | 36 | 1 | 3 |
| β-strand | 54-56 | 3 | 4 |
| β-strand | 61 | 1 | 3 |
| β-strand | 62-64 | 3 | 4 |
| β-strand | 66-68 | 3 | 2 |
| α-helix | 73-82 | 10 | |
| α-helix | 89-91 | 3 | |
| α-helix | 105-114 | 10 | |
| α-helix | 116-128 | 13 | |
| β-strand | 133 | 1 | 1 |
| β-strand | 136-141 | 6 | 2 |
| α-helix | 145-151 | 7 | |
| α-helix | 152-161 | 10 | |
| β-strand | 167-172 | 6 | 2 |
| α-helix | 180-197 | 18 | |
| β-strand | 200 | 1 | 2 |
| β-strand | 201-202 | 2 | 5 |
| β-strand | 203-204 | 2 | 2 |
| α-helix | 206-216 | 11 | |
| α-helix | 227-234 | 8 | |
| α-helix | 240-243 | 4 | |
| α-helix | 253-259 | 7 | |
| α-helix | 263-265 | 3 | |
| β-strand | 267-268 | 2 | 5 |
| β-strand | 269-272 | 4 | 6 |
| β-strand | 289 | 1 | 7 |
| α-helix | 291-296 | 6 | |
| α-helix | 301-303 | 3 | |
| β-strand | 304 | 1 | 6 |
| β-strand | 314 | 1 | 8 |
| β-strand | 315-324 | 10 | 6 |
| α-helix | 328-334 | 7 | |
| α-helix | 336-339 | 4 | |
| β-strand | 343 | 1 | 8 |
| α-helix | 344 | 1 | |
| β-strand | 353-356 | 4 | 6 |
| α-helix | 364-366 | 3 | |
| β-strand | 371 | 1 | 7 |
| β-strand | 372-380 | 9 | 6 |
| α-helix | 384-386 | 3 | |
| α-helix | 388-398 | 11 | |
| α-helix | 405-407 | 3 | |
| α-helix | 411-414 | 4 | |
| α-helix | 416-439 | 24 | |
| α-helix | 443-451 | 9 | |
Chain B: 26 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-10 | 7 | 9 |
| α-helix | 13-28 | 16 | |
| β-strand | 36 | 1 | 10 |
| β-strand | 54-56 | 3 | 11 |
| β-strand | 61 | 1 | 10 |
| β-strand | 62-64 | 3 | 11 |
| β-strand | 66-70 | 5 | 9 |
| α-helix | 73-80 | 8 | |
| α-helix | 89-91 | 3 | |
| β-strand | 92-94 | 3 | 9 |
| α-helix | 98-101 | 4 | |
| α-helix | 104-114 | 11 | |
| α-helix | 116-127 | 12 | |
| β-strand | 133-140 | 8 | 9 |
| α-helix | 145-161 | 17 | |
| β-strand | 166-172 | 7 | 9 |
| α-helix | 184-194 | 11 | |
| β-strand | 201-204 | 4 | 9 |
| α-helix | 207-216 | 10 | |
| α-helix | 224-226 | 3 | |
| α-helix | 228-236 | 9 | |
| α-helix | 237-239 | 3 | |
| α-helix | 240-243 | 4 | |
| α-helix | 252-259 | 8 | |
| β-strand | 268 | 1 | 9 |
| β-strand | 269-272 | 4 | 12 |
| α-helix | 291-296 | 6 | |
| α-helix | 297-299 | 3 | |
| α-helix | 301-303 | 3 | |
| β-strand | 304 | 1 | 12 |
| α-helix | 313-314 | 2 | |
| β-strand | 315-323 | 9 | 12 |
| α-helix | 330-339 | 10 | |
| α-helix | 346-348 | 3 | |
| α-helix | 350-352 | 3 | |
| β-strand | 353-356 | 4 | 12 |
| α-helix | 364-366 | 3 | |
| β-strand | 373-380 | 8 | 12 |
| α-helix | 381-385 | 5 | |
| α-helix | 388-398 | 11 | |
| α-helix | 416-439 | 24 | |
| α-helix | 444-446 | 3 | |
Chain C: 35 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 167-171 | 5 | |
| α-helix | 172-174 | 3 | |
| α-helix | 179-180 | 2 | |
| α-helix | 181-192 | 12 | |
| β-strand | 202 | 1 | 13 |
| α-helix | 206 | 1 | |
| β-strand | 207-209 | 3 | 13 |
| α-helix | 215-242 | 28 | |
| α-helix | 248-273 | 26 | |
| α-helix | 280-300 | 21 | |
| α-helix | 304-306 | 3 | |
| α-helix | 309-319 | 11 | |
| α-helix | 325-347 | 23 | |
| α-helix | 348-352 | 5 | |
| β-strand | 364-366 | 3 | 14 |
| β-strand | 383-385 | 3 | 14 |
| α-helix | 387-389 | 3 | |
| α-helix | 396-410 | 15 | |
| α-helix | 411-416 | 6 | |
| α-helix | 419-434 | 16 | |
| α-helix | 443-466 | 24 | |
| α-helix | 470-481 | 12 | |
| α-helix | 486-495 | 10 | |
| α-helix | 497-501 | 5 | |
| β-strand | 504 | 1 | 15 |
| α-helix | 509-522 | 14 | |
| α-helix | 526-529 | 4 | |
| α-helix | 536-540 | 5 | |
| β-strand | 541-545 | 5 | 16 |
| β-strand | 552 | 1 | 15 |
| α-helix | 555-557 | 3 | |
| β-strand | 558-562 | 5 | 16 |
| α-helix | 569-572 | 4 | |
| α-helix | 583-614 | 32 | |
| α-helix | 622-626 | 5 | |
| α-helix | 629-652 | 24 | |
| α-helix | 653-657 | 5 | |
| α-helix | 658-669 | 12 | |
| β-strand | 681-683 | 3 | 17 |
| α-helix | 684 | 1 | |
| β-strand | 689-691 | 3 | 17 |
| α-helix | 721-736 | 16 | |
| α-helix | 759-789 | 31 | |
| α-helix | 801-831 | 31 | |
| α-helix | 836-844 | 9 | |
Chain D: 44 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3 | 1 | 18 |
| β-strand | 8-10 | 3 | 13 |
| β-strand | 12 | 1 | 19 |
| β-strand | 26 | 1 | 19 |
| α-helix | 29-31 | 3 | |
| β-strand | 38 | 1 | 18 |
| α-helix | 44-46 | 3 | |
| α-helix | 52-66 | 15 | |
| β-strand | 75-77 | 3 | 20 |
| β-strand | 92-94 | 3 | 20 |
| α-helix | 100-125 | 26 | |
| α-helix | 133-145 | 13 | |
| 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 | 226-228 | 3 | |
| β-strand | 232-235 | 4 | 21 |
| α-helix | 237-239 | 3 | |
| α-helix | 245-257 | 13 | |
| α-helix | 262-289 | 28 | |
| β-strand | 301-303 | 3 | 21 |
| β-strand | 324-327 | 4 | 21 |
| α-helix | 328-330 | 3 | |
| α-helix | 338-361 | 24 | |
| α-helix | 376-378 | 3 | |
| α-helix | 381-385 | 5 | |
| α-helix | 389-407 | 19 | |
| α-helix | 408-412 | 5 | |
| α-helix | 415-426 | 12 | |
| α-helix | 432-446 | 15 | |
| α-helix | 449-451 | 3 | |
| α-helix | 458-470 | 13 | |
| α-helix | 477-480 | 4 | |
| β-strand | 482-486 | 5 | 22 |
| α-helix | 491-494 | 4 | |
| α-helix | 495-497 | 3 | |
| α-helix | 502-504 | 3 | |
| β-strand | 560-564 | 5 | 22 |
| α-helix | 568-571 | 4 | |
| α-helix | 576-606 | 31 | |
| α-helix | 610-613 | 4 | |
| α-helix | 619-621 | 3 | |
| 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 | 717-720 | 4 | |
| α-helix | 722-724 | 3 | |
| α-helix | 754-785 | 32 | |
| α-helix | 802-809 | 8 | |
Chain U: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 119-139 | 21 | |
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) |
| Spindle pole body component 110 | U | protein | 220 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P32380 (AlphaFold model) |
Sequence of entity 1 (A, B), FASTA
>7M2Y_1 Tubulin gamma chain (chains A, B)
MGGEIITLQAGQCGNHVGKFLWSQLAKEHAIGTDGLSQLPDSSTERDDDTKPFFRENSRN
KFTPRAIMMDSEPSVIADVENTFRGFFDPRNTWVASDGASAGNSWANGYDIGTRNQDDIL
NKIDKEIDSTDNFEGFQLLHSVAGGTGSGLGSNLLEALCDRYPKKILTTYSVFPARSSEV
VVQSYNTILALRRLIEDSDATVVFDNASLLNISGKVFRNPNIDLQHTNQLISTIISSVTN
SIRFPSYMYSSMSSIYSTLIPSPELHFLSPSFTPFTSDYIHDDIAHKGHSSYDVMLDLLD
PSNSLVSTAMNNPTYFNVYNTIIGNVEPRQISRAMTKLQQRIKFPSWSSSAMHVNIGRRS
PYLPLQPNENEVSGMMLSNMSTVVNVFENACNTFDKVFAKGAFLNNYNVGDLFQSMQNVQ
DEFAESREVVQSLMEDYVAAEQDSYLDDVLVDDENMVGELEEDLDADGDHKLV
Sequence of entity 2 (C), FASTA
>7M2Y_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
>7M2Y_3 Spindle pole body component SPC97 (chains D)
MEIKEVDDRAELLRYTNNIPLLGKLVNHQPLWSTNPKLKSFSLEKISAPDQRRVQEALVV
KDLLNVLIGLEGTYIRYFNDYEPSDPETPIEFKIAKKMDPSFKTFSRRIVRYGKQYMILT
RAYEKWSDTSFGMVLQRFAYEIRRFLEDVYLKTLVERLERDFNKVPNFSIRELEQIINET
EVNKQMELLYNIYEEIFREIEERRTNQSSQEDFNNFMDSMKNESSLHLRLMVAFDTTVYP
VPKGGAILKIFQQKILENLGDRSSVMFLKKLLNNISQDYCTMLYEWLTQGILNDPYQEFM
TYDDLEGKTDNIFDTRDRAWDTQYFIRKDVLLRDCDSEEDKNLLFKMLRTGILLKVVRAS
LQIPTIPSNSSDITIQEINDFADLMEGSNLELYVDKCYSRANEIFLKLFFQGYDLINVLK
HLQQIFLGYQSGHNVLKFLTKNMGELTKHYRNDNNANYDKLLQNFELERQSENPNNLMRQ
LLMIQFDTETLPQVLSHYLQIYPEVPENNSANDDSDPLMHANNFKNMNAILFDELSKERT
GAYHGSNLELYTPKSAIYHLKFDINIPYPLNIIISRTCMIKYQIILRYQLVLQYHSRLLD
ETWMDLNKTPSWKYRGYSHTVKRRIVRATRVLHAKMNHFIKTIMEYFNQNVIDKEVYSLE
KCYRNPTLAVAIQNELEGGLTNIMTNRCLSDLIPLQLQIFDIVYKFCKFIKSMRAKLCQL
DPVLYEKHKSGMMKTLNEGYRTNNGGQEDVGYQEDAALELIQKLIEYISNASSIFRKCLI
NFTQELSTEKFDFYDSSSVDAAGIERVLYSIVPPRSASASSQR
Sequence of entity 4 (U), FASTA
>7M2Y_4 Spindle pole body component 110 (chains U)
MDEASHLPNGSLKNMEFTPVGFIKSKRNTTQTQVVSPTKVPNANNGDENEGPVKKRQRRS
IDDTIDSTRLFSEASQFDDSFPEIKANIPPSPRSGNVDKSRKRNLIDDLKKDVPMSQPLK
EQEVREHQMKKERFDRALESKLLGKRHITYANSDISNKELYINEIKSLKHEIKELRKEKN
DTLNNYDTLEEETDDLKNRLQALEKELDAKNKIVNSRKVD
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
- 7M2Z 3.7 Å, Monomeric single-particle reconstruction of the Yeast gamma-TuSC
- 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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