3BZC

Crystal Structure of the Tex protein from Pseudomonas aeruginosa, crystal form I

3BZC の概要

• エントリーDOI: 10.2210/pdb3bzc/pdb
• 関連するPDBエントリー: 3BZK
• 分子名称: Tex (2 entities in total)
• 機能のキーワード: helix-turn-helix, helix-hairpin-helix, s1 domain, yqgf domain, transcription, rna binding protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 85910.95

構造登録者

Johnson, S.J.,Close, D.,Hill, C.P. (登録日: 2008-01-17, 公開日: 2008-04-08, 最終更新日: 2024-02-21)

主引用文献

Johnson, S.J.,Close, D.,Robinson, H.,Vallet-Gely, I.,Dove, S.L.,Hill, C.P.
Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa.
J.Mol.Biol., 377:1460-1473, 2008

PubMed Abstract: Tex is a highly conserved bacterial protein that likely functions in a variety of transcriptional processes. Here, we describe two crystal structures of the 86-kDa Tex protein from Pseudomonas aeruginosa at 2.3 and 2.5 A resolution, respectively. These structures reveal a relatively flat and elongated protein, with several potential nucleic acid binding motifs clustered at one end, including an S1 domain near the C-terminus that displays considerable structural flexibility. Tex binds nucleic acids, with a preference for single-stranded RNA, and the Tex S1 domain is required for this binding activity. Point mutants further demonstrate that the primary nucleic acid binding site corresponds to a surface of the S1 domain. Sequence alignment and modeling indicate that the eukaryotic Spt6 transcription factor adopts a similar core structure. Structural analysis further suggests that the RNA polymerase and nucleosome interacting regions of Spt6 flank opposite sides of the Tex-like scaffold. Therefore, the Tex structure may represent a conserved scaffold that binds single-stranded RNA to regulate transcription in both eukaryotic and prokaryotic organisms.

PubMed: 18321528
DOI: 10.1016/j.jmb.2008.01.096

実験手法

X-RAY DIFFRACTION (2.27 Å)