Ontology highlight
ABSTRACT:
SUBMITTER: Johnson SJ
PROVIDER: S-EPMC2680229 | biostudies-literature | 2008 Apr
REPOSITORIES: biostudies-literature
Johnson Sean J SJ Close Devin D Robinson Howard H Vallet-Gely Isabelle I Dove Simon L SL Hill Christopher P CP
Journal of molecular biology 20080212 5
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 aci ...[more]