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-Structure paper
タイトル | MZT Proteins Form Multi-Faceted Structural Modules in the γ-Tubulin Ring Complex. |
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ジャーナル・号・ページ | Cell Rep, Vol. 31, Issue 13, Page 107791, Year 2020 |
掲載日 | 2020年6月30日 |
著者 | Michal Wieczorek / Tzu-Lun Huang / Linas Urnavicius / Kuo-Chiang Hsia / Tarun M Kapoor / |
PubMed 要旨 | Microtubule organization depends on the γ-tubulin ring complex (γ-TuRC), a ∼2.3-MDa nucleation factor comprising an asymmetric assembly of γ-tubulin and GCP2-GCP6. However, it is currently ...Microtubule organization depends on the γ-tubulin ring complex (γ-TuRC), a ∼2.3-MDa nucleation factor comprising an asymmetric assembly of γ-tubulin and GCP2-GCP6. However, it is currently unclear how the γ-TuRC-associated microproteins MZT1 and MZT2 contribute to the structure and regulation of the holocomplex. Here, we report cryo-EM structures of MZT1 and MZT2 in the context of the native human γ-TuRC. MZT1 forms two subcomplexes with the N-terminal α-helical domains of GCP3 or GCP6 (GCP-NHDs) within the γ-TuRC "lumenal bridge." We determine the X-ray structure of recombinant MZT1/GCP6-NHD and find it is similar to that within the native γ-TuRC. We identify two additional MZT/GCP-NHD-like subcomplexes, one of which is located on the outer face of the γ-TuRC and comprises MZT2 and GCP2-NHD in complex with a centrosomin motif 1 (CM1)-containing peptide. Our data reveal how MZT1 and MZT2 establish multi-faceted, structurally mimetic "modules" that can expand structural and regulatory interfaces in the γ-TuRC. |
リンク | Cell Rep / PubMed:32610146 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 3.29434890409 - 4.5 Å |
構造データ | EMDB-21984, PDB-6x0u: EMDB-21985, PDB-6x0v: PDB-6m33: |
由来 |
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キーワード | CELL CYCLE / Gamma tubulin complex / microtubule / GCP / Mzt1 / STRUCTURAL PROTEIN / gamma-TuRC / lumenal bridge / MZT2 / CDK5Rap2 |