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| | <StructureSection load='4pcb' size='340' side='right'caption='[[4pcb]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='4pcb' size='340' side='right'caption='[[4pcb]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pcb]] 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=4PCB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PCB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pcb]] 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=4PCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PCB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1omh|1omh]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pcb OCA], [https://pdbe.org/4pcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pcb RCSB], [https://www.ebi.ac.uk/pdbsum/4pcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pcb ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trwC ([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=4pcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pcb OCA], [http://pdbe.org/4pcb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pcb RCSB], [http://www.ebi.ac.uk/pdbsum/4pcb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pcb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q47673_ECOLX Q47673_ECOLX] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Carballeira, J D]] | + | [[Category: Carballeira JD]] |
| - | [[Category: Cruz, F de la]]
| + | [[Category: Gonzalez-Perez B]] |
| - | [[Category: Gonzalez-Perez, B]] | + | [[Category: Moncalian G]] |
| - | [[Category: Moncalian, G]] | + | [[Category: De la Cruz F]] |
| - | [[Category: Huh endonuclease]] | + | |
| - | [[Category: Plasmid conjugation]]
| + | |
| - | [[Category: Relaxase]]
| + | |
| - | [[Category: Transferase-dna complex]]
| + | |
| Structural highlights
Function
Q47673_ECOLX
Publication Abstract from PubMed
Relaxases act as DNA selection sieves in conjugative plasmid transfer. Most plasmid relaxases belong to the HUH endonuclease family. TrwC, the relaxase of plasmid R388, is the prototype of the HUH relaxase family, which also includes TraI of plasmid F. In this article we demonstrate that TrwC processes its target nic-site by means of a highly secure double lock and key mechanism. It is controlled both by TrwC-DNA intermolecular interactions and by intramolecular DNA interactions between several nic nucleotides. The sequence specificity map of the interaction between TrwC and DNA was determined by systematic mutagenesis using degenerate oligonucleotide libraries. The specificity map reveals the minimal nic sequence requirements for R388-based conjugation. Some nic-site sequence variants were still able to form the U-turn shape at the nic-site necessary for TrwC processing, as observed by X-ray crystallography. Moreover, purified TrwC relaxase effectively cleaved ssDNA as well as dsDNA substrates containing these mutant sequences. Since TrwC is able to catalyze DNA integration in a nic-site-containing DNA molecule, characterization of nic-site functionally active sequence variants should improve the search quality of potential target sequences for relaxase-mediated integration in any target genome.
A high security double lock and key mechanism in HUH relaxases controls oriT-processing for plasmid conjugation.,Carballeira JD, Gonzalez-Perez B, Moncalian G, la Cruz Fd Nucleic Acids Res. 2014 Dec 1;42(16):10632-43. doi: 10.1093/nar/gku741. Epub 2014, Aug 14. PMID:25123661[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Carballeira JD, Gonzalez-Perez B, Moncalian G, la Cruz Fd. A high security double lock and key mechanism in HUH relaxases controls oriT-processing for plasmid conjugation. Nucleic Acids Res. 2014 Dec 1;42(16):10632-43. doi: 10.1093/nar/gku741. Epub 2014, Aug 14. PMID:25123661 doi:http://dx.doi.org/10.1093/nar/gku741
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