3bzk: Difference between revisions

Revision as of 00:12, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3bzk.png

Template:STRUCTURE 3bzk

Crystal Structure of the Tex protein from Pseudomonas aeruginosa, crystal form 2Crystal Structure of the Tex protein from Pseudomonas aeruginosa, crystal form 2

Template:ABSTRACT PUBMED 18321528

About this StructureAbout this Structure

3BZK is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa., Johnson SJ, Close D, Robinson H, Vallet-Gely I, Dove SL, Hill CP, J Mol Biol. 2008 Apr 11;377(5):1460-73. Epub 2008 Feb 12. PMID:18321528

Page seeded by OCA on Tue Jul 29 00:12:23 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of the Tex protein from Pseudomonas aeruginosa, crystal form 2'''
+===Crystal Structure of the Tex protein from Pseudomonas aeruginosa, crystal form 2===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18321528}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_18321528}}
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 [[Category: Transcription]]
 [[Category: Yqgf domain]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:12:23 2008''