PDBsum entry 3bzc

RNA binding protein

PDB id: 3bzc

Contents

Protein chain

730 a.a. *

Waters ×73

* Residue conservation analysis

PDB id:

3bzc

Name:

RNA binding protein

Title:

Crystal structure of the tex protein from pseudomonas aeruginosa, crystal form i

Structure:

Tex. Chain: a. Engineered: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 287. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.27Å R-factor: 0.288 R-free: 0.274

Authors:

S.J.Johnson,D.Close,C.P.Hill

Key ref:

S.J.Johnson et al. (2008). Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa. J Mol Biol, 377, 1460-1473. PubMed id: 18321528 DOI: 10.1016/j.jmb.2008.01.096

Date:

17-Jan-08 Release date: 08-Apr-08

Protein chain

Q9HTY8  (Q9HTY8_PSEAE) -  S1 motif domain-containing protein from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 779 a.a.

Struc: 730 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jmb.2008.01.096

J Mol Biol 377:1460-1473 (2008)

PubMed id: 18321528

Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa.

S.J.Johnson, D.Close, H.Robinson, I.Vallet-Gely, S.L.Dove, C.P.Hill.

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.

Selected figure(s)

Figure 2.
Fig. 2. Tex domain arrangement. (a and b) Orthogonal views of ribbon diagram of the Tex structure. Structural motifs identified from primary sequence and structural analyses are colored. Blue, HtH motif. Red, YqgF homologous domain. Yellow, tandem HhH motif. Green, S1 domain. (c) Tex domain structure, colored as in (a) and (b). The segment boxed with broken lines, comprising residues 1–730, indicates the region of Tex sequence observed in the crystal structure.

Figure 9.
Fig. 9. Model for Spt6 structure. (a) Comparison of Tex (top) and Spt6 (bottom) domain structures. (b) The Tex structure is used to model the central portion of the Spt6 structure (surface representation). A proposed nucleosome-binding domain (magenta, inset) is modeled based on structural alignment with the C-terminal portion of the ISWI nucleosome interacting domain (PDB accession code: 1OFC). An SH2-like domain (orange, PDB accession code: 1PIC) is modeled at the C-terminal end of the S1 domain.

The above figures are reprinted from an Open Access publication published by Elsevier: J Mol Biol (2008, 377, 1460-1473) copyright 2008.

Figures were selected by an automated process.