Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Partial closure of the γ-tubulin ring complex by CDK5RAP2 activates microtubule nucleation.
Journal, issue, pages	Dev Cell, Year 2024
Publish date	Sep 23, 2024
Authors	Yixin Xu / Hugo Muñoz-Hernández / Rościsław Krutyhołowa / Florina Marxer / Ferdane Cetin / Michal Wieczorek /
PubMed Abstract	Microtubule nucleation is templated by the γ-tubulin ring complex (γ-TuRC), but its structure deviates from the geometry of α-/β-tubulin in the microtubule, explaining the complex's poor ...Microtubule nucleation is templated by the γ-tubulin ring complex (γ-TuRC), but its structure deviates from the geometry of α-/β-tubulin in the microtubule, explaining the complex's poor nucleating activity. Several proteins may activate the γ-TuRC, but the mechanisms underlying activation are not known. Here, we determined the structure of the porcine γ-TuRC purified using CDK5RAP2's centrosomin motif 1 (CM1). We identified an unexpected conformation of the γ-TuRC bound to multiple protein modules containing MZT2, GCP2, and CDK5RAP2, resulting in a long-range constriction of the γ-tubulin ring that brings it in closer agreement with the 13-protofilament microtubule. Additional CDK5RAP2 promoted γ-TuRC decoration and stimulated the microtubule-nucleating activities of the porcine γ-TuRC and a reconstituted, CM1-free human complex in single-molecule assays. Our results provide a structural mechanism for the control of microtubule nucleation by CM1 proteins and identify conformational transitions in the γ-TuRC that prime it for microtubule nucleation.
External links	Dev Cell / PubMed:39321808
Methods	EM (single particle)
Resolution	4.0 - 7.5 Å
Structure data	EMDB-51007: Structure of the Position 1 to 3 Open gamma-Tubulin Ring Complex from Pig Brain Method: EM (single particle) / Resolution: 5.8 Å EMDB-51008: Structure of the Position 4 to 11 Open gamma-Tubulin Ring Complex from Pig Brain Method: EM (single particle) / Resolution: 4.37 Å EMDB-51010: Structure of the Position 10 to 12 Open gamma-Tubulin Ring Complex from Pig Brain Method: EM (single particle) / Resolution: 4.9 Å EMDB-51011: Structure of the Position 1 to 3 CMG-decorated gamma-Tubulin Ring Complex from Pig Brain Method: EM (single particle) / Resolution: 7.5 Å EMDB-51012: Structure of the Position 4 to 7 CMG-decorated gamma-Tubulin Ring Complex from Pig Brain Method: EM (single particle) / Resolution: 4.5 Å EMDB-51013: Structure of the Position 13 to 14 CMG-decorated gamma-Tubulin Ring Complex from Pig Brain Method: EM (single particle) / Resolution: 7.5 Å EMDB-51014: Structure of the Position 10 to 12 CMG-decorated gamma-Tubulin Ring Complex from Pig Brain Method: EM (single particle) / Resolution: 7.0 Å EMDB-51015: Structure of the Position 8 to 9 CMG-decorated gamma-Tubulin Ring Complex from Pig Brain Method: EM (single particle) / Resolution: 4.6 Å EMDB-51016: Consensus cryo-EM reconstruction of the S. scrofa gamma-TuRC Method: EM (single particle) / Resolution: 4.0 Å 51017 9g3x EMDB-51017, PDB-9g3x: Structure of the Partially-assembled gamma-Tubulin Ring Complex from Pig Brain Method: EM (single particle) / Resolution: 4.5 Å 51018 9g3y EMDB-51018, PDB-9g3y: Structure of the Native CMG-decorated gamma-Tubulin Ring Complex from Pig Brain Method: EM (single particle) / Resolution: 6.8 Å 51019 9g3z EMDB-51019, PDB-9g3z: Structure of the Open gamma-Tubulin Ring Complex from Pig Brain Method: EM (single particle) / Resolution: 4.3 Å 51020 9g40 EMDB-51020, PDB-9g40: Structure of the Position 7 CMG-decorated gamma-Tubulin Ring Complex from Pig Brain Method: EM (single particle) / Resolution: 4.3 Å
Source	sus scrofa (pig) homo sapiens (human)
Keywords	STRUCTURAL PROTEIN / Tubulin Complex