1u78
From Proteopedia
Line 4: | Line 4: | ||
|PDB= 1u78 |SIZE=350|CAPTION= <scene name='initialview01'>1u78</scene>, resolution 2.69Å | |PDB= 1u78 |SIZE=350|CAPTION= <scene name='initialview01'>1u78</scene>, resolution 2.69Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= | + | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Tc3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans]) | |GENE= Tc3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1tc3|1TC3]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u78 OCA], [http://www.ebi.ac.uk/pdbsum/1u78 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u78 RCSB]</span> | ||
}} | }} | ||
Line 30: | Line 33: | ||
[[Category: transposon dna]] | [[Category: transposon dna]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:06:21 2008'' |
Revision as of 21:06, 30 March 2008
| |||||||
, resolution 2.69Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | , , , | ||||||
Gene: | Tc3 (Caenorhabditis elegans) | ||||||
Related: | 1TC3
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structure of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA
Overview
The bipartite DNA-binding domain of Tc3 transposase, Tc3A, was crystallized in complex with its transposon recognition sequence. In the structure the two DNA-binding domains form structurally related helix-turn-helix (HTH) motifs. They both bind to the major groove on a single DNA oligomer, separated by a linker that interacts closely with the minor groove. The structure resembles that of the transcription factor Pax6 DNA-binding domain, but the relative orientation of the HTH-domain is different. The DNA conformation is distorted, characterized by local narrowing of the minor groove and bends at both ends. The protein-DNA recognition takes place through base and backbone contacts, as well as shape-recognition of the distortions in the DNA. Charged interactions are primarily found in the N-terminal domain and the linker indicating that these may form the initial contact area. Two independent dimer interfaces could be relevant for bringing together transposon ends and for binding to a direct repeat site in the transposon end. In contrast to the Tn5 synaptic complex, the two Tc3A DNA-binding domains bind to a single Tc3 transposon end.
About this Structure
1U78 is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.
Reference
Structural analysis of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA., Watkins S, van Pouderoyen G, Sixma TK, Nucleic Acids Res. 2004 Aug 10;32(14):4306-12. Print 2004. PMID:15304566
Page seeded by OCA on Mon Mar 31 00:06:21 2008