7RGU

The crystal structure of RocC bound to a transcriptional terminator

7RGU の概要

• エントリーDOI: 10.2210/pdb7rgu/pdb
• 分子名称: Repressor of competence, RNA Chaperone, Modified SL3 of RocR (2 entities in total)
• 機能のキーワード: rna chaperone, rna binding protein, fino, proq, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Legionella pneumophila; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 168216.27

構造登録者

Kim, H.J.,Edwards, R.A.,Glover, J.N.M. (登録日: 2021-07-15, 公開日: 2022-11-09, 最終更新日: 2024-04-03)

主引用文献

Kim, H.J.,Black, M.,Edwards, R.A.,Peillard-Fiorente, F.,Panigrahi, R.,Klingler, D.,Eidelpes, R.,Zeindl, R.,Peng, S.,Su, J.,Omar, A.R.,MacMillan, A.M.,Kreutz, C.,Tollinger, M.,Charpentier, X.,Attaiech, L.,Glover, J.N.M.
Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones.
Nat Commun, 13:7076-7076, 2022

PubMed Abstract: The ProQ/FinO family of RNA binding proteins mediate sRNA-directed gene regulation throughout gram-negative bacteria. Here, we investigate the structural basis for RNA recognition by ProQ/FinO proteins, through the crystal structure of the ProQ/FinO domain of the Legionella pneumophila DNA uptake regulator, RocC, bound to the transcriptional terminator of its primary partner, the sRNA RocR. The structure reveals specific recognition of the 3' nucleotide of the terminator by a conserved pocket involving a β-turn-α-helix motif, while the hairpin portion of the terminator is recognized by a conserved α-helical N-cap motif. Structure-guided mutagenesis reveals key RNA contact residues that are critical for RocC/RocR to repress the uptake of environmental DNA in L. pneumophila. Structural analysis and RNA binding studies reveal that other ProQ/FinO domains also recognize related transcriptional terminators with different specificities for the length of the 3' ssRNA tail.

PubMed: 36400772
DOI: 10.1038/s41467-022-34875-5

実験手法

X-RAY DIFFRACTION (3.2 Å)