8cvt

Human 19S-20S proteasome, state SD2

spinqualitylabelsall models 8cvt, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8cvt is a 14 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 3Å Ligands: ATP, LDZ, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PRS7_HUMAN The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. In case of HIV-1 infection, positive modulator of Tat-mediated transactivation. Publication Abstract from PubMed The ability to produce folded and functional proteins is a necessity for structural biology and many other biological sciences. This task is particularly challenging for numerous biomedically important targets in human cells, including membrane proteins and large macromolecular assemblies, hampering mechanistic studies and drug development efforts. Here we describe a method combining CRISPR-Cas gene editing and fluorescence-activated cell sorting to rapidly tag and purify endogenous proteins in HEK cells for structural characterization. We applied this approach to study the human proteasome from HEK cells and rapidly determined cryogenic electron microscopy structures of major proteasomal complexes, including a high-resolution structure of intact human PA28alphabeta-20S. Our structures reveal that PA28 with a subunit stoichiometry of 3alpha/4beta engages tightly with the 20S proteasome. Addition of a hydrophilic peptide shows that polypeptides entering through PA28 are held in the antechamber of 20S prior to degradation in the proteolytic chamber. This study provides critical insights into an important proteasome complex and demonstrates key methodologies for the tagging of proteins from endogenous sources. Structural insights into the human PA28-20S proteasome enabled by efficient tagging and purification of endogenous proteins.,Zhao J, Makhija S, Zhou C, Zhang H, Wang Y, Muralidharan M, Huang B, Cheng Y Proc Natl Acad Sci U S A. 2022 Aug 16;119(33):e2207200119. doi: , 10.1073/pnas.2207200119. Epub 2022 Jul 19. PMID:35858375 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thyroid hormone receptor 3D structures

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