6M33
Crystal structure of Homo Sapian GCP6 N-terminus and Mozart1
Summary for 6M33
| Entry DOI | 10.2210/pdb6m33/pdb |
| Descriptor | Gamma-tubulin complex component 6, Mitotic-spindle organizing protein 1 (2 entities in total) |
| Functional Keywords | gamma tubulin complex, microtubule, gcp, mzt1, cell cycle |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 22353.85 |
| Authors | Huang, T.L.,Hsia, K.C. (deposition date: 2020-03-02, release date: 2021-02-03, Last modification date: 2024-03-27) |
| Primary citation | Wieczorek, M.,Huang, T.L.,Urnavicius, L.,Hsia, K.C.,Kapoor, T.M. MZT Proteins Form Multi-Faceted Structural Modules in the gamma-Tubulin Ring Complex. Cell Rep, 31:107791-107791, 2020 Cited by PubMed Abstract: 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. PubMed: 32610146DOI: 10.1016/j.celrep.2020.107791 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.29434890409 Å) |
Structure validation
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