1t0f

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(New page: 200px<br /><applet load="1t0f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t0f, resolution 1.85&Aring;" /> '''Crystal Structure of...)
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[[Image:1t0f.gif|left|200px]]<br /><applet load="1t0f" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1t0f, resolution 1.85&Aring;" />
 
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'''Crystal Structure of the TnsA/TnsC(504-555) complex'''<br />
 
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==Overview==
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==Crystal Structure of the TnsA/TnsC(504-555) complex==
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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.
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<StructureSection load='1t0f' size='340' side='right'caption='[[1t0f]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1t0f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T0F FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0f OCA], [https://pdbe.org/1t0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t0f RCSB], [https://www.ebi.ac.uk/pdbsum/1t0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0f ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TNSA_ECOLX TNSA_ECOLX] Required for Tn7 transposition. Forms the transposase, together with TnsB. TnsA executes the 5'-DNA strand breakage reaction. TnsABC and TnsD promote high-frequency insertion of Tn7 into a specific target site known as ATT-Tn7 whereas TnsABC and TnsD promote low-frequency insertion into many different sites.<ref>PMID:8947057</ref> <ref>PMID:10704304</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t0/1t0f_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t0f ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:15257292</ref>
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1T0F is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, MLA and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T0F OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15257292 15257292]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1t0f" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Craig, N.L.]]
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[[Category: Dyda, F.]]
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[[Category: Hickman, A.B.]]
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[[Category: Li, Y.]]
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[[Category: Perez, Z.N.]]
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[[Category: Ronning, D.R.]]
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[[Category: Ross, P.D.]]
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[[Category: MG]]
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[[Category: MLA]]
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[[Category: MPD]]
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[[Category: mixed alpha-beta]]
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[[Category: protein-protein complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:53:33 2007''
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==See Also==
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*[[Transposase 3D structures|Transposase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Craig NL]]
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[[Category: Dyda F]]
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[[Category: Hickman AB]]
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[[Category: Li Y]]
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[[Category: Perez ZN]]
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[[Category: Ronning DR]]
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[[Category: Ross PD]]

Current revision

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

PDB ID 1t0f

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