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1t0f

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Revision as of 11:38, 24 December 2020

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

Structural highlights

1t0f is a 4 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1f1z
Gene:	TNSA ("Bacillus coli" Migula 1895), TNSC ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] [TNSC_ECOLX] TnsC binds non-specifically to DNA in the presence of ATP. It is required for Tn7 transposition. TnsABC + TnsD promote high-frequency insertion of Tn7 into a specific target site known as att-Tn7 whereas TnsABC + TnsE promote low-frequency insertion into many different sites.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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 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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sarnovsky RJ, May EW, Craig NL. The Tn7 transposase is a heteromeric complex in which DNA breakage and joining activities are distributed between different gene products. EMBO J. 1996 Nov 15;15(22):6348-61. PMID:8947057
↑ Biery MC, Lopata M, Craig NL. A minimal system for Tn7 transposition: the transposon-encoded proteins TnsA and TnsB can execute DNA breakage and joining reactions that generate circularized Tn7 species. J Mol Biol. 2000 Mar 17;297(1):25-37. PMID:10704304 doi:http://dx.doi.org/10.1006/jmbi.2000.3558
↑ Ronning DR, Li Y, Perez ZN, Ross PD, Hickman AB, Craig NL, Dyda F. The carboxy-terminal portion of TnsC activates the Tn7 transposase through a specific interaction with TnsA. EMBO J. 2004 Aug 4;23(15):2972-81. Epub 2004 Jul 15. PMID:15257292 doi:http://dx.doi.org/10.1038/sj.emboj.7600311

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t0f"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the TnsA/TnsC(504-555) complex==
-<StructureSection load='1t0f' size='340' side='right' caption='[[1t0f]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+<StructureSection load='1t0f' size='340' side='right'caption='[[1t0f]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1t0f]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T0F FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1t0f]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1T0F FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
+</td></tr><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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f1z|1f1z]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f1z|1f1z]]</div></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TNSA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), TNSC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1t0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t0f RCSB], [http://www.ebi.ac.uk/pdbsum/1t0f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0f ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0f OCA], [http://pdbe.org/1t0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t0f RCSB], [http://www.ebi.ac.uk/pdbsum/1t0f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0f ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 30: / Line 30: @@
 </div>
 <div class="pdbe-citations 1t0f" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Transposase 3D structures|Transposase 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 38: @@
 </StructureSection>
 [[Category: Bacillus coli migula 1895]]
+[[Category: Large Structures]]
 [[Category: Craig, N L]]
 [[Category: Dyda, F]]

1t0f

From Proteopedia

Revision as of 11:38, 24 December 2020

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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