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	Negative charge in the RACK1 loop broadens the translational capacity of the human ribosome.
Journal, issue, pages	Cell Rep, Vol. 36, Issue 10, Page 109663, Year 2021
Publish date	Sep 7, 2021
Authors	Madeline G Rollins / Manidip Shasmal / Nathan Meade / Helen Astar / Peter S Shen / Derek Walsh /
PubMed Abstract	Although the roles of initiation factors, RNA binding proteins, and RNA elements in regulating translation are well defined, how the ribosome functionally diversifies remains poorly understood. In ...Although the roles of initiation factors, RNA binding proteins, and RNA elements in regulating translation are well defined, how the ribosome functionally diversifies remains poorly understood. In their human hosts, poxviruses phosphorylate serine 278 (S) at the tip of a loop domain in the small subunit ribosomal protein RACK1, thereby mimicking negatively charged residues in the RACK1 loops of dicot plants and protists to stimulate translation of transcripts with 5' poly(A) leaders. However, how a negatively charged RACK1 loop affects ribosome structure and its broader translational output is not known. Here, we show that although ribotoxin-induced stress signaling and stalling on poly(A) sequences are unaffected, negative charge in the RACK1 loop alters the swivel motion of the 40S head domain in a manner similar to several internal ribosome entry sites (IRESs), confers resistance to various protein synthesis inhibitors, and broadly supports noncanonical modes of translation.
External links	Cell Rep / PubMed:34496247 / PubMed Central
Methods	EM (single particle)
Resolution	3.0 - 5.2 Å
Structure data	EMDB-24541: RACK1-S278E 80S rotated state, consensus reconstruction Method: EM (single particle) / Resolution: 3.1 Å EMDB-24542: RACK1-S278E, 80S non-rotated state, consensus reconstruction Method: EM (single particle) / Resolution: 3.9 Å EMDB-24544: RACK1-S278E, reconstruction from 40S particles (filtered according to local resolution) Method: EM (single particle) / Resolution: 5.2 Å EMDB-24545: RACK1-WT, 80S rotated state, consensus reconstruction Method: EM (single particle) / Resolution: 4.2 Å EMDB-24548: RACK1-WT, 80S nonrotated consensus reconstruction Method: EM (single particle) / Resolution: 5.0 Å EMDB-24549: RACK1-S278E, 60S masked from 80S rotated state, locally refined and filtered Method: EM (single particle) / Resolution: 3.0 Å EMDB-24552: RACK1-S278E, 40S body masked from 80S rotated state, locally refined and filtered Method: EM (single particle) / Resolution: 3.2 Å EMDB-24553: RACK1-S278E, 40S head masked from 80S rotated state, locally refined and filtered Method: EM (single particle) / Resolution: 3.3 Å EMDB-24554: RACK1-WT, 60S masked from 80S rotated state, locally refined and filtered Method: EM (single particle) / Resolution: 3.9 Å EMDB-24556: RACK1-WT, 40S body masked from 80S rotated state, locally refined and filtered Method: EM (single particle) / Resolution: 4.4 Å EMDB-24557: RACK1-WT, 40S head masked from 80S rotated state, locally refined and filtered Method: EM (single particle) / Resolution: 4.5 Å
Source	Homo sapiens (human)