2R1C

Coordinates of the thermus thermophilus ribosome binding factor A (RbfA) homology model as fitted into the CRYO-EM map of a 30S-RBFA complex

Summary for 2R1C

• Entry DOI: 10.2210/pdb2r1c/pdb
• Related: 1JOS 2DYJ 2R1G
• EMDB information: 1413
• Descriptor: Ribosome-binding factor A (1 entity in total)
• Functional Keywords: helix-kink-helix, kh domain, rrna processing, rna binding protein
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 10875.71

Authors

Datta, P.P.,Wilson, D.N.,Kawazoe, M.,Swami, N.K.,Kaminishi, T.,Sharma, M.R.,Booth, T.M.,Takemoto, C.,Fucini, P.,Yokoyama, S.,Agrawal, R.K. (deposition date: 2007-08-22, release date: 2008-03-18, Last modification date: 2024-03-13)

Primary citation

Datta, P.P.,Wilson, D.N.,Kawazoe, M.,Swami, N.K.,Kaminishi, T.,Sharma, M.R.,Booth, T.M.,Takemoto, C.,Fucini, P.,Yokoyama, S.,Agrawal, R.K.
Structural aspects of RbfA action during small ribosomal subunit assembly.
Mol.Cell, 28:434-445, 2007

PubMed Abstract: Ribosome binding factor A (RbfA) is a bacterial cold shock response protein, required for an efficient processing of the 5' end of the 16S ribosomal RNA (rRNA) during assembly of the small (30S) ribosomal subunit. Here we present a crystal structure of Thermus thermophilus (Tth) RbfA and a three-dimensional cryo-electron microscopic (EM) map of the Tth 30S*RbfA complex. RbfA binds to the 30S subunit in a position overlapping the binding sites of the A and P site tRNAs, and RbfA's functionally important C terminus extends toward the 5' end of the 16S rRNA. In the presence of RbfA, a portion of the 16S rRNA encompassing helix 44, which is known to be directly involved in mRNA decoding and tRNA binding, is displaced. These results shed light on the role played by RbfA during maturation of the 30S subunit, and also indicate how RbfA provides cells with a translational advantage under conditions of cold shock.

PubMed: 17996707
DOI: 10.1016/j.molcel.2007.08.026

Experimental method

ELECTRON MICROSCOPY (12.5 Å)