7M2X: Tubulin gamma chain
Open conformation of the Yeast wild-type gamma-TuRC. Determined by electron microscopy at 3.6 Å resolution. Released 12 May 2021.
- Method
- Electron microscopy
- Resolution
- 3.6 Å
- Organism
- Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
- Chains
- 5
- Atoms
- 18,704
- Mol. weight
- 326.96 kDa
- Ligands
- GDP
- Released
- 12 May 2021
Explore 7M2X in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7M2X contains 128 α-helices and 58 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: 22 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-10 | 7 | 1 |
| α-helix | 11-28 | 18 | |
| β-strand | 31 | 1 | 2 |
| β-strand | 37 | 1 | 2 |
| β-strand | 54-56 | 3 | 3 |
| β-strand | 62-64 | 3 | 3 |
| β-strand | 66-70 | 5 | 1 |
| α-helix | 73-80 | 8 | |
| α-helix | 89-91 | 3 | |
| β-strand | 92-94 | 3 | 1 |
| α-helix | 105-114 | 10 | |
| α-helix | 116-127 | 12 | |
| β-strand | 133-141 | 9 | 1 |
| α-helix | 145-161 | 17 | |
| β-strand | 166-173 | 8 | 1 |
| α-helix | 174-176 | 3 | |
| α-helix | 180-197 | 18 | |
| β-strand | 201-205 | 5 | 1 |
| α-helix | 206-216 | 11 | |
| α-helix | 228-238 | 11 | |
| α-helix | 240-243 | 4 | |
| α-helix | 252-256 | 5 | |
| β-strand | 267-268 | 2 | 1 |
| β-strand | 269-273 | 5 | 4 |
| α-helix | 291-298 | 8 | |
| α-helix | 301-303 | 3 | |
| β-strand | 304 | 1 | 4 |
| β-strand | 315-323 | 9 | 4 |
| α-helix | 328-338 | 11 | |
| β-strand | 353-357 | 5 | 4 |
| α-helix | 366-368 | 3 | |
| β-strand | 373-380 | 8 | 4 |
| α-helix | 383-387 | 5 | |
| α-helix | 388-397 | 10 | |
| α-helix | 402-405 | 4 | |
| α-helix | 410-413 | 4 | |
| α-helix | 417-439 | 23 | |
| α-helix | 444-450 | 7 | |
Chain B: 21 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-9 | 6 | 5 |
| α-helix | 12-28 | 17 | |
| β-strand | 31 | 1 | 6 |
| β-strand | 36 | 1 | 7 |
| β-strand | 37 | 1 | 6 |
| β-strand | 54-56 | 3 | 8 |
| β-strand | 61 | 1 | 7 |
| β-strand | 62-64 | 3 | 8 |
| β-strand | 66-70 | 5 | 5 |
| α-helix | 73-82 | 10 | |
| α-helix | 89-91 | 3 | |
| β-strand | 92-94 | 3 | 5 |
| α-helix | 95-96 | 2 | |
| α-helix | 104-114 | 11 | |
| α-helix | 116-127 | 12 | |
| β-strand | 133-139 | 7 | 5 |
| α-helix | 145-161 | 17 | |
| β-strand | 167-173 | 7 | 5 |
| α-helix | 180-197 | 18 | |
| β-strand | 200-205 | 6 | 5 |
| α-helix | 206-216 | 11 | |
| α-helix | 224-238 | 15 | |
| α-helix | 240-243 | 4 | |
| α-helix | 252-259 | 8 | |
| β-strand | 267-268 | 2 | 5 |
| β-strand | 269-273 | 5 | 9 |
| α-helix | 291-298 | 8 | |
| α-helix | 301-303 | 3 | |
| β-strand | 304 | 1 | 9 |
| β-strand | 318-321 | 4 | 9 |
| α-helix | 328-341 | 14 | |
| β-strand | 352-355 | 4 | 9 |
| α-helix | 358-360 | 3 | |
| α-helix | 364-365 | 2 | |
| α-helix | 368-370 | 3 | |
| β-strand | 374-378 | 5 | 9 |
| α-helix | 384-400 | 17 | |
| α-helix | 419-439 | 21 | |
| α-helix | 447-450 | 4 | |
Chain C: 46 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3 | 1 | 10 |
| β-strand | 9-10 | 2 | 11 |
| β-strand | 12 | 1 | 12 |
| β-strand | 26 | 1 | 12 |
| α-helix | 27-31 | 5 | |
| β-strand | 38 | 1 | 10 |
| α-helix | 43-46 | 4 | |
| α-helix | 52-67 | 16 | |
| β-strand | 75-77 | 3 | 13 |
| β-strand | 92-94 | 3 | 13 |
| α-helix | 100-125 | 26 | |
| α-helix | 129-131 | 3 | |
| 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 | |
| β-strand | 232-235 | 4 | 14 |
| α-helix | 237-239 | 3 | |
| α-helix | 245-255 | 11 | |
| α-helix | 262-273 | 12 | |
| α-helix | 277-289 | 13 | |
| β-strand | 302 | 1 | 14 |
| α-helix | 322-323 | 2 | |
| β-strand | 324-327 | 4 | 14 |
| α-helix | 328-330 | 3 | |
| α-helix | 338-361 | 24 | |
| α-helix | 368-370 | 3 | |
| α-helix | 376-378 | 3 | |
| α-helix | 381-384 | 4 | |
| α-helix | 389-407 | 19 | |
| α-helix | 408-412 | 5 | |
| α-helix | 415-426 | 12 | |
| α-helix | 432-441 | 10 | |
| α-helix | 443-445 | 3 | |
| α-helix | 459-469 | 11 | |
| α-helix | 477-480 | 4 | |
| β-strand | 482-486 | 5 | 15 |
| α-helix | 491-498 | 8 | |
| β-strand | 560-564 | 5 | 15 |
| α-helix | 566-567 | 2 | |
| α-helix | 570-572 | 3 | |
| α-helix | 576-608 | 33 | |
| α-helix | 619-621 | 3 | |
| α-helix | 622-627 | 6 | |
| α-helix | 628-647 | 20 | |
| α-helix | 648-652 | 5 | |
| α-helix | 653-663 | 11 | |
| α-helix | 669-684 | 16 | |
| α-helix | 687-690 | 4 | |
| α-helix | 693-709 | 17 | |
| α-helix | 712-716 | 5 | |
| α-helix | 717-720 | 4 | |
| α-helix | 722-725 | 4 | |
| α-helix | 755-787 | 33 | |
| α-helix | 802-811 | 10 | |
Chain D: 38 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 167-171 | 5 | |
| α-helix | 172-174 | 3 | |
| α-helix | 181-191 | 11 | |
| β-strand | 202 | 1 | 11 |
| β-strand | 207-208 | 2 | 11 |
| α-helix | 209-210 | 2 | |
| α-helix | 215-242 | 28 | |
| α-helix | 248-274 | 27 | |
| α-helix | 280-300 | 21 | |
| α-helix | 301-303 | 3 | |
| α-helix | 309-319 | 11 | |
| α-helix | 325-347 | 23 | |
| α-helix | 348-352 | 5 | |
| β-strand | 364-366 | 3 | 16 |
| β-strand | 383-385 | 3 | 16 |
| α-helix | 387-389 | 3 | |
| α-helix | 396-410 | 15 | |
| α-helix | 411-415 | 5 | |
| α-helix | 419-435 | 17 | |
| α-helix | 437-439 | 3 | |
| α-helix | 444-464 | 21 | |
| α-helix | 470-480 | 11 | |
| α-helix | 486-495 | 10 | |
| α-helix | 497-501 | 5 | |
| β-strand | 503 | 1 | 17 |
| α-helix | 504-506 | 3 | |
| α-helix | 511-521 | 11 | |
| α-helix | 526-529 | 4 | |
| α-helix | 535-538 | 4 | |
| β-strand | 541-542 | 2 | 18 |
| β-strand | 545 | 1 | 19 |
| β-strand | 553 | 1 | 17 |
| α-helix | 554-557 | 4 | |
| β-strand | 558 | 1 | 19 |
| β-strand | 561-562 | 2 | 18 |
| α-helix | 582-611 | 30 | |
| α-helix | 616-619 | 4 | |
| α-helix | 621-623 | 3 | |
| α-helix | 625-652 | 28 | |
| α-helix | 653-657 | 5 | |
| α-helix | 658-668 | 11 | |
| α-helix | 670-672 | 3 | |
| β-strand | 681-683 | 3 | 20 |
| β-strand | 689-691 | 3 | 20 |
| α-helix | 694-697 | 4 | |
| α-helix | 721-735 | 15 | |
| α-helix | 739-741 | 3 | |
| α-helix | 758-792 | 35 | |
| α-helix | 799-831 | 33 | |
| α-helix | 836-844 | 9 | |
Chain U: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 119-141 | 23 | |
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 SPC97 | C | protein | 823 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P38863 (AlphaFold model) |
| Spindle pole body component SPC98 | D | protein | 846 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P53540 (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
>7M2X_1 Tubulin gamma chain (chains A, B)
MGGEIITLQAGQCGNHVGKFLWSQLAKEHAIGTDGLSQLPDSSTERDDDTKPFFRENSRN
KFTPRAIMMDSEPSVIADVENTFRGFFDPRNTWVASDGASAGNSWANGYDIGTRNQDDIL
NKIDKEIDSTDNFEGFQLLHSVAGGTGSGLGSNLLEALCDRYPKKILTTYSVFPARSSEV
VVQSYNTILALRRLIEDSDATVVFDNASLLNISGKVFRNPNIDLQHTNQLISTIISSVTN
SIRFPSYMYSSMSSIYSTLIPSPELHFLSPSFTPFTSDYIHDDIAHKGHSSYDVMLDLLD
PSNSLVSTAMNNPTYFNVYNTIIGNVEPRQISRAMTKLQQRIKFPSWSSSAMHVNIGRRS
PYLPLQPNENEVSGMMLSNMSTVVNVFENACNTFDKVFAKGAFLNNYNVGDLFQSMQNVQ
DEFAESREVVQSLMEDYVAAEQDSYLDDVLVDDENMVGELEEDLDADGDHKLV
Sequence of entity 2 (C), FASTA
>7M2X_2 Spindle pole body component SPC97 (chains C)
MEIKEVDDRAELLRYTNNIPLLGKLVNHQPLWSTNPKLKSFSLEKISAPDQRRVQEALVV
KDLLNVLIGLEGTYIRYFNDYEPSDPETPIEFKIAKKMDPSFKTFSRRIVRYGKQYMILT
RAYEKWSDTSFGMVLQRFAYEIRRFLEDVYLKTLVERLERDFNKVPNFSIRELEQIINET
EVNKQMELLYNIYEEIFREIEERRTNQSSQEDFNNFMDSMKNESSLHLRLMVAFDTTVYP
VPKGGAILKIFQQKILENLGDRSSVMFLKKLLNNISQDYCTMLYEWLTQGILNDPYQEFM
TYDDLEGKTDNIFDTRDRAWDTQYFIRKDVLLRDCDSEEDKNLLFKMLRTGILLKVVRAS
LQIPTIPSNSSDITIQEINDFADLMEGSNLELYVDKCYSRANEIFLKLFFQGYDLINVLK
HLQQIFLGYQSGHNVLKFLTKNMGELTKHYRNDNNANYDKLLQNFELERQSENPNNLMRQ
LLMIQFDTETLPQVLSHYLQIYPEVPENNSANDDSDPLMHANNFKNMNAILFDELSKERT
GAYHGSNLELYTPKSAIYHLKFDINIPYPLNIIISRTCMIKYQIILRYQLVLQYHSRLLD
ETWMDLNKTPSWKYRGYSHTVKRRIVRATRVLHAKMNHFIKTIMEYFNQNVIDKEVYSLE
KCYRNPTLAVAIQNELEGGLTNIMTNRCLSDLIPLQLQIFDIVYKFCKFIKSMRAKLCQL
DPVLYEKHKSGMMKTLNEGYRTNNGGQEDVGYQEDAALELIQKLIEYISNASSIFRKCLI
NFTQELSTEKFDFYDSSSVDAAGIERVLYSIVPPRSASASSQR
Sequence of entity 3 (D), FASTA
>7M2X_3 Spindle pole body component SPC98 (chains D)
MELEPTLFGIIEALAPQLLSQSHLQTFVSDVVNLLRSSTKSATQLGPLIDFYKLQSLDSP
ETTIMWHKIEKFLDALFGIQNTDDMVKYLSVFQSLLPSNYRAKIVQKSSGLNMENLANHE
HLLSPVRAPSIYTEASFENMDRFSERRSMVSSPNRYVPSSTYSSVTLRQLSNPYYVNTIP
EEDILKYVSYTLLATTSALFPFDHEQIQIPSKIPNFESGLLHLIFEAGLLYQSLGYKVEK
FRMLNISPMKKALIIEISEELQNYTAFVNNLVSSGTVVSLKSLYREIYENIIRLRIYCRF
TEHLEELSGDTFLIELNIFKSHGDLTIRKIATNLFNSMISLYYEYLMNWLTKGLLRATYG
EFFIAENTDTNGTDDDFIYHIPIEFNQERVPAFIPKELAYKIFMIGKSYIFLEKYCKEVQ
WTNEFSKKYHVLYQSNSYRGISTNFFEIINDQYSEIVNHTNQILNQKFHYRDVVFALKNI
LLMGKSDFMDALIEKANDILATPSDSLPNYKLTRVLQEAVQLSSLRHLMNSPRNSSVING
LDARVLDLGHGSVGWDVFTLDYILYPPLSLVLNVNRPFGRKEYLRIFNFLWRFKKNNYFY
QKEMLKSNDIIRSFKKIRGYNPLIRDIINKLSRISILRTQFQQFNSKMESYYLNCIIEEN
FKEMTRKLQRTENKSQNQFDLIRLNNGTIELNGILTPKAEVLTKSSSSKPQKHAIEKTLN
IDELESVHNTFLTNILSHKLFATNTSEISVGDYSGQPYPTSLVLLLNSVYEFVKVYCNLN
DIGYEIFIKMNLNDHEASNGLLGKFNTNLKEIVSQYKNFKDRLYIFRADLKNDGDEELFL
LSKSLR
Sequence of entity 4 (U), FASTA
>7M2X_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)
- 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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