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	Structural insights into the assembly of the 30S ribosomal subunit in vivo: functional role of S5 and location of the 17S rRNA precursor sequence.
Journal, issue, pages	Protein Cell, Vol. 5, Issue 5, Page 394-407, Year 2014
Publish date	Mar 28, 2014
Authors	Zhixiu Yang / Qiang Guo / Simon Goto / Yuling Chen / Ningning Li / Kaige Yan / Yixiao Zhang / Akira Muto / Haiteng Deng / Hyouta Himeno / Jianlin Lei / Ning Gao /
PubMed Abstract	The in vivo assembly of ribosomal subunits is a highly complex process, with a tight coordination between protein assembly and rRNA maturation events, such as folding and processing of rRNA ...The in vivo assembly of ribosomal subunits is a highly complex process, with a tight coordination between protein assembly and rRNA maturation events, such as folding and processing of rRNA precursors, as well as modifications of selected bases. In the cell, a large number of factors are required to ensure the efficiency and fidelity of subunit production. Here we characterize the immature 30S subunits accumulated in a factor-null Escherichia coli strain (∆rsgA∆rbfA). The immature 30S subunits isolated with varying salt concentrations in the buffer system show interesting differences on both protein composition and structure. Specifically, intermediates derived under the two contrasting salt conditions (high and low) likely reflect two distinctive assembly stages, the relatively early and late stages of the 3' domain assembly, respectively. Detailed structural analysis demonstrates a mechanistic coupling between the maturation of the 5' end of the 17S rRNA and the assembly of the 30S head domain, and attributes a unique role of S5 in coordinating these two events. Furthermore, our structural results likely reveal the location of the unprocessed terminal sequences of the 17S rRNA, and suggest that the maturation events of the 17S rRNA could be employed as quality control mechanisms on subunit production and protein translation.
External links	Protein Cell / PubMed:24671761 / PubMed Central
Methods	EM (single particle)
Resolution	13.5 - 21.2 Å
Structure data	EMDB-5900: Cryo-EM structure of low salt treated immature 30S ribosomal subunit from rsga and rbfa deleted E.coli strain Method: EM (single particle) / Resolution: 15.2 Å EMDB-5904: Cryo-EM structure of low salt treated immature 30S ribosomal subunit from rsga and rbfa deleted E.coli strain Method: EM (single particle) / Resolution: 13.5 Å EMDB-5905: Cryo-EM structure of low salt treated immature 30S ribosomal subunit from rsga and rbfa deleted E.coli strain Method: EM (single particle) / Resolution: 14.4 Å EMDB-5906: Cryo-EM structure of low salt treated immature 30S ribosomal subunit from rsga and rbfa deleted E.coli strain Method: EM (single particle) / Resolution: 17.8 Å EMDB-5907: Cryo-EM structure of low salt treated immature 30S ribosomal subunit from rsga and rbfa deleted E.coli strain Method: EM (single particle) / Resolution: 14.3 Å EMDB-5908: Cryo-EM structure of high salt treated immature 30S ribosomal subunit from rsga and rbfa deleted E.coli strain Method: EM (single particle) / Resolution: 21.2 Å EMDB-5909: Cryo-EM structure of high salt treated immature 30S ribosomal subunit from rsga and rbfa deleted E.coli strain Method: EM (single particle) / Resolution: 15.2 Å EMDB-5910: Cryo-EM structure of high salt treated immature 30S ribosomal subunit from rsga and rbfa deleted E.coli strain Method: EM (single particle) / Resolution: 18.3 Å
Source	Escherichia coli (E. coli)