3RIP

Crystal Structure of human gamma-tubulin complex protein 4 (GCP4)

Summary for 3RIP

• Entry DOI: 10.2210/pdb3rip/pdb
• Descriptor: Gamma-tubulin complex component 4, (4R)-2-METHYLPENTANE-2,4-DIOL, GLYCEROL, ... (4 entities in total)
• Functional Keywords: helix bundles, gamma-tubulin ring complex, gamma-turc, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton, centrosome: Q9UGJ1
• Total number of polymer chains: 1
• Total formula weight: 78352.39

Authors

Gregory-Pauron, L.,Guillet, V.,Mourey, L. (deposition date: 2011-04-14, release date: 2011-07-06, Last modification date: 2024-11-27)

Primary citation

Guillet, V.,Knibiehler, M.,Gregory-Pauron, L.,Remy, M.H.,Chemin, C.,Raynaud-Messina, B.,Bon, C.,Kollman, J.M.,Agard, D.A.,Merdes, A.,Mourey, L.
Crystal structure of gamma-tubulin complex protein GCP4 provides insight into microtubule nucleation.
Nat.Struct.Mol.Biol., 18:915-919, 2011

PubMed Abstract: Microtubule nucleation in all eukaryotes involves γ-tubulin small complexes (γTuSCs) that comprise two molecules of γ-tubulin bound to γ-tubulin complex proteins (GCPs) GCP2 and GCP3. In many eukaryotes, multiple γTuSCs associate with GCP4, GCP5 and GCP6 into large γ-tubulin ring complexes (γTuRCs). Recent cryo-EM studies indicate that a scaffold similar to γTuRCs is formed by lateral association of γTuSCs, with the C-terminal regions of GCP2 and GCP3 binding γ-tubulin molecules. However, the exact role of GCPs in microtubule nucleation remains unknown. Here we report the crystal structure of human GCP4 and show that its C-terminal domain binds directly to γ-tubulin. The human GCP4 structure is the prototype for all GCPs, as it can be precisely positioned within the γTuSC envelope, revealing the nature of protein-protein interactions and conformational changes regulating nucleation activity.

PubMed: 21725292
DOI: 10.1038/nsmb.2083

Experimental method

X-RAY DIFFRACTION (2.3 Å)