1t0f
From Proteopedia
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|PDB= 1t0f |SIZE=350|CAPTION= <scene name='initialview01'>1t0f</scene>, resolution 1.85Å | |PDB= 1t0f |SIZE=350|CAPTION= <scene name='initialview01'>1t0f</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene> | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|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]) | |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]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1f1z|1F1Z]] | ||
| + | |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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[[Category: Ronning, D R.]] | [[Category: Ronning, D R.]] | ||
[[Category: Ross, P D.]] | [[Category: Ross, P D.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: MLA]] | ||
| - | [[Category: MPD]] | ||
[[Category: mixed alpha-beta]] | [[Category: mixed alpha-beta]] | ||
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:25 2008'' |
Revision as of 20:49, 30 March 2008
| |||||||
| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | TNSA (Escherichia coli), TNSC (Escherichia coli) | ||||||
| Related: | 1F1Z
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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