3BZC
Crystal Structure of the Tex protein from Pseudomonas aeruginosa, crystal form I
Summary for 3BZC
| Entry DOI | 10.2210/pdb3bzc/pdb |
| Related | 3BZK |
| Descriptor | Tex (2 entities in total) |
| Functional Keywords | helix-turn-helix, helix-hairpin-helix, s1 domain, yqgf domain, transcription, rna binding protein |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 1 |
| Total formula weight | 85910.95 |
| Authors | Johnson, S.J.,Close, D.,Hill, C.P. (deposition date: 2008-01-17, release date: 2008-04-08, Last modification date: 2024-02-21) |
| Primary citation | 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 Cited by 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: 18321528DOI: 10.1016/j.jmb.2008.01.096 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.27 Å) |
Structure validation
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