1t0f: Difference between revisions

Revision as of 19:00, 28 July 2008

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File:1t0f.png

Template:STRUCTURE 1t0f

Crystal Structure of the TnsA/TnsC(504-555) complexCrystal Structure of the TnsA/TnsC(504-555) complex

Template:ABSTRACT PUBMED 15257292

About this StructureAbout this Structure

1T0F is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

The carboxy-terminal portion of TnsC activates the Tn7 transposase through a specific interaction with TnsA., Ronning DR, Li Y, Perez ZN, Ross PD, Hickman AB, Craig NL, Dyda F, EMBO J. 2004 Aug 4;23(15):2972-81. Epub 2004 Jul 15. PMID:15257292

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OCA

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-'''Crystal Structure of the TnsA/TnsC(504-555) complex'''
+===Crystal Structure of the TnsA/TnsC(504-555) complex===
-==Overview==
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-Tn7 transposition requires the assembly of a nucleoprotein complex containing four self-encoded proteins, transposon ends, and target DNA. Within this complex, TnsC, the molecular switch that regulates transposition, and TnsA, one part of the transposase, interact directly. Here, we demonstrate that residues 504-555 of TnsC are responsible for TnsA/TnsC interaction. The crystal structure of the TnsA/TnsC(504-555) complex, resolved to 1.85 A, illustrates the burial of a large hydrophobic patch on the surface of TnsA. One consequence of sequestering this patch is a marked increase in the thermal stability of TnsA as shown by differential scanning calorimetry. A model based on the complex structure suggested that TnsA and a slightly longer version of the cocrystallized TnsC fragment (residues 495-555) might cooperate to bind DNA, a prediction confirmed using gel mobility shift assays. Donor DNA binding by the TnsA/TnsC(495-555) complex is correlated with the activation of the TnsAB transposase, as measured by double-stranded DNA cleavage assays, demonstrating the importance of the TnsA/TnsC interaction in affecting Tn7 transposition.
+The line below this paragraph, {{ABSTRACT_PUBMED_15257292}}, adds the Publication Abstract to the page
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 [[Category: Mixed alpha-beta]]
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