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6X0V

Structure of MZT2/GCP-NHD and CDK5Rap2 at position 13 of the gamma-TuRC

Summary for 6X0V
Entry DOI10.2210/pdb6x0v/pdb
Related6X0U
EMDB information21984 21985
DescriptorMitotic-spindle organizing protein 2A, Gamma-tubulin complex component 2, Centrosome protein Cep215 (3 entities in total)
Functional Keywordsgamma-turc, mzt2, gcp, cdk5rap2, structural protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight552841.01
Authors
Wieczorek, M.,Huang, T.-L.,Urnavicius, L.,Hsia, K.-C.,Kapoor, T.M. (deposition date: 2020-05-17, release date: 2020-07-22, Last modification date: 2024-03-06)
Primary citationWieczorek, 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: 32610146
DOI: 10.1016/j.celrep.2020.107791
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.5 Å)
Structure validation

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