3R2D

Crystal Structure of Antitermination Factors NusB and NusE in complex with dsRNA

Summary for 3R2D

• Entry DOI: 10.2210/pdb3r2d/pdb
• Related: 3R2C
• Descriptor: N utilization substance protein B, 30S ribosomal protein S10, 5'-R(*GP*GP*CP*UP*CP*CP*UP*UP*GP*GP*CP*A)-3', ... (5 entities in total)
• Functional Keywords: cross species nusb-nuse-rna interaction, transcription elongation, gene regulation, protein-rna interaction, transcription-rna complex, transcription/rna
• Biological source: Aquifex aeolicus; More
• Total number of polymer chains: 6
• Total formula weight: 61803.73

Authors

Stagno, J.R.,Ji, X. (deposition date: 2011-03-14, release date: 2011-06-22, Last modification date: 2023-09-13)

Primary citation

Stagno, J.R.,Altieri, A.S.,Bubunenko, M.,Tarasov, S.G.,Li, J.,Court, D.L.,Byrd, R.A.,Ji, X.
Structural basis for RNA recognition by NusB and NusE in the initiation of transcription antitermination.
Nucleic Acids Res., 39:7803-7815, 2011

PubMed Abstract: Processive transcription antitermination requires the assembly of the complete antitermination complex, which is initiated by the formation of the ternary NusB-NusE-BoxA RNA complex. We have elucidated the crystal structure of this complex, demonstrating that the BoxA RNA is composed of 8 nt that are recognized by the NusB-NusE heterodimer. Functional biologic and biophysical data support the structural observations and establish the relative significance of key protein-protein and protein-RNA interactions. Further crystallographic investigation of a NusB-NusE-dsRNA complex reveals a heretofore unobserved dsRNA binding site contiguous with the BoxA binding site. We propose that the observed dsRNA represents BoxB RNA, as both single-stranded BoxA and double-stranded BoxB components are present in the classical lambda antitermination site. Combining these data with known interactions amongst antitermination factors suggests a specific model for the assembly of the complete antitermination complex.

PubMed: 21652641
DOI: 10.1093/nar/gkr418

Experimental method

X-RAY DIFFRACTION (2.199 Å)