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	Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle.
Journal, issue, pages	Mol Cell, Vol. 67, Issue 2, Page 322-333.e6, Year 2017
Publish date	Jul 20, 2017
Authors	Ying Lu / Jiayi Wu / Yuanchen Dong / Shuobing Chen / Shuangwu Sun / Yong-Bei Ma / Qi Ouyang / Daniel Finley / Marc W Kirschner / Youdong Mao /
PubMed Abstract	The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of ...The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembly chaperones in mammals: PAAF1, p28/gankyrin, p27/PSMD9, and S5b. Using cryogenic electron microscopy, we analyzed the non-AAA structure of the p28-bound human RP at 4.5 Å resolution and determined seven distinct conformations of the Rpn1-p28-AAA subcomplex within the p28-bound RP at subnanometer resolutions. Remarkably, the p28-bound AAA ring does not form a channel in the free RP and spontaneously samples multiple "open" and "closed" topologies at the Rpt2-Rpt6 and Rpt3-Rpt4 interfaces. Our analysis suggests that p28 assists the proteolytic core particle to select a specific conformation of the ATPase ring for RP engagement and is released in a shoehorn-like fashion in the last step of the chaperone-mediated proteasome assembly.
External links	Mol Cell / PubMed:28689658 / PubMed Central
Methods	EM (single particle)
Resolution	4.5 - 8.9 Å
Structure data	8672 5vgz EMDB-8672, PDB-5vgz: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Method: EM (single particle) / Resolution: 4.5 Å 8674 5vhf EMDB-8674, PDB-5vhf: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Method: EM (single particle) / Resolution: 5.7 Å 8675 5vhh EMDB-8675, PDB-5vhh: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Method: EM (single particle) / Resolution: 6.1 Å 8676 5vhi EMDB-8676, PDB-5vhi: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Method: EM (single particle) / Resolution: 6.8 Å 8677 5vhj EMDB-8677, PDB-5vhj: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Method: EM (single particle) / Resolution: 8.5 Å 8678 5vhm EMDB-8678, PDB-5vhm: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Method: EM (single particle) / Resolution: 8.3 Å 8679 5vhn EMDB-8679, PDB-5vhn: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Method: EM (single particle) / Resolution: 7.3 Å 8680 5vho EMDB-8680, PDB-5vho: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Method: EM (single particle) / Resolution: 8.3 Å 8681 5vhp EMDB-8681, PDB-5vhp: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Method: EM (single particle) / Resolution: 7.9 Å 8682 5vhq EMDB-8682, PDB-5vhq: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Method: EM (single particle) / Resolution: 8.9 Å 8683 5vhr EMDB-8683, PDB-5vhr: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Method: EM (single particle) / Resolution: 7.7 Å 8684 5vhs EMDB-8684, PDB-5vhs: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Method: EM (single particle) / Resolution: 8.8 Å
Chemicals	ChemComp-ZN: Unknown entry
Source	homo sapiens (human)
Keywords	HYDROLASE / p28 / 26S proteasome / regulatory particle / 19S / gankyrin