8shq

CCT G beta 5 complex closed state 12

spinqualitylabelsall models 8shq, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8shq is a 18 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.9Å Ligands: ADP, AF3, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHLP_HUMAN Acts as a positive regulator of hedgehog signaling and regulates ciliary function.[UniProtKB:Q9DBX2] Functions as a co-chaperone for CCT in the assembly of heterotrimeric G protein complexes, facilitates the assembly of both Gbeta-Ggamma and RGS-Gbeta5 heterodimers. Acts as a negative regulator of heterotrimeric G proteins assembly by trapping the preloaded G beta subunits inside the CCT chaperonin. Publication Abstract from PubMed The Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential protein folding machine with a diverse clientele of substrates, including many proteins with beta-propeller domains. Here, we determine the structures of human CCT in complex with its accessory co-chaperone, phosducin-like protein 1 (PhLP1), in the process of folding Gbeta(5), a component of Regulator of G protein Signaling (RGS) complexes. Cryoelectron microscopy (cryo-EM) and image processing reveal an ensemble of distinct snapshots that represent the folding trajectory of Gbeta(5) from an unfolded molten globule to a fully folded beta-propeller. These structures reveal the mechanism by which CCT directs Gbeta(5) folding through initiating specific intermolecular contacts that facilitate the sequential folding of individual beta sheets until the propeller closes into its native structure. This work directly visualizes chaperone-mediated protein folding and establishes that CCT orchestrates folding by stabilizing intermediates through interactions with surface residues that permit the hydrophobic core to coalesce into its folded state. Visualizing the chaperone-mediated folding trajectory of the G protein beta5 beta-propeller.,Wang S, Sass MI, Kwon Y, Ludlam WG, Smith TM, Carter EJ, Gladden NE, Riggi M, Iwasa JH, Willardson BM, Shen PS Mol Cell. 2023 Nov 2;83(21):3852-3868.e6. doi: 10.1016/j.molcel.2023.09.032. Epub , 2023 Oct 17. PMID:37852256 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transducin 3D structures

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