1t0f

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[[Image:1t0f.gif|left|200px]]
[[Image:1t0f.gif|left|200px]]
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{{Structure
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|PDB= 1t0f |SIZE=350|CAPTION= <scene name='initialview01'>1t0f</scene>, resolution 1.85&Aring;
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The line below this paragraph, containing "STRUCTURE_1t0f", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= TNSA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), TNSC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1t0f| PDB=1t0f | SCENE= }}
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|RELATEDENTRY=[[1f1z|1F1Z]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0f OCA], [http://www.ebi.ac.uk/pdbsum/1t0f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t0f RCSB]</span>
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'''Crystal Structure of the TnsA/TnsC(504-555) complex'''
'''Crystal Structure of the TnsA/TnsC(504-555) complex'''
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[[Category: Ronning, D R.]]
[[Category: Ronning, D R.]]
[[Category: Ross, P D.]]
[[Category: Ross, P D.]]
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[[Category: mixed alpha-beta]]
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[[Category: Mixed alpha-beta]]
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[[Category: protein-protein complex]]
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[[Category: Protein-protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:20:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:25 2008''
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Revision as of 06:20, 3 May 2008

Image:1t0f.gif

Template:STRUCTURE 1t0f

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


Overview

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.

About this Structure

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

Reference

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 Page seeded by OCA on Sat May 3 09:20:52 2008

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