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6L81

Crystal structure of Homo sapiens GCP5 N-terminus and Mozart1

Summary for 6L81
Entry DOI10.2210/pdb6l81/pdb
DescriptorGamma-tubulin complex component 5, Mitotic-spindle organizing protein 1 (3 entities in total)
Functional Keywordsgamma tubulin complex, microprotein, microtubule, translation
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight45858.17
Authors
Huang, T.L.,Wang, H.J.,Wang, S.W.,Hsia, K.C. (deposition date: 2019-11-04, release date: 2020-07-15, Last modification date: 2024-03-27)
Primary citationHuang, T.L.,Wang, H.J.,Chang, Y.C.,Wang, S.W.,Hsia, K.C.
Promiscuous Binding of Microprotein Mozart1 to gamma-Tubulin Complex Mediates Specific Subcellular Targeting to Control Microtubule Array Formation.
Cell Rep, 31:107836-107836, 2020
Cited by
PubMed Abstract: How γ-tubulin ring complex (γ-TuRC), a master template for microtubule nucleation, is spatially and temporally regulated for the assembly of new microtubule arrays remains unclear. Here, we report that an evolutionarily conserved microprotein, Mozart1 (Mzt1), regulates subcellular targeting and microtubule formation activity of γ-TuRC at different cell cycle stages. Crystal structures of protein complexes demonstrate that Mzt1 promiscuously interacts with the N-terminal domains of multiple γ-tubulin complex protein subunits in γ-TuRC via an intercalative binding mode. Genetic- and microscopy-based analyses show that promiscuous binding of Mzt1 in γ-TuRC controls specific subcellular localization of γ-TuRC to modulate microtubule nucleation and stabilization in fission yeast. Moreover, we find Mzt1-independent targeting of γ-TuRC to be crucial for mitotic spindle assembly, demonstrating the cell-cycle-dependent regulation and function of γ-TuRC. Our findings reveal a microprotein-mediated regulatory mechanism underlying microtubule cytoskeleton formation, whereby Mzt1 binding promiscuity confers localization specificity on the multi-protein complex γ-TuRC.
PubMed: 32610137
DOI: 10.1016/j.celrep.2020.107836
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.19650999049 Å)
Structure validation

229380

건을2024-12-25부터공개중

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