4lvk
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lvk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LVK FirstGlance]. <br> | <table><tr><td colspan='2'>[[4lvk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LVK FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.37Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=4lvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvk OCA], [https://pdbe.org/4lvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lvk RCSB], [https://www.ebi.ac.uk/pdbsum/4lvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lvk ProSAT]</span></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=4lvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvk OCA], [https://pdbe.org/4lvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lvk RCSB], [https://www.ebi.ac.uk/pdbsum/4lvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lvk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PRE_STRAG PRE_STRAG] The interaction of the RSA site and the PRE protein may not only serves a function in plasmid maintenance, but may also contributes to the distribution of small antibiotic resistance plasmids among Gram-positive bacteria. | [https://www.uniprot.org/uniprot/PRE_STRAG PRE_STRAG] The interaction of the RSA site and the PRE protein may not only serves a function in plasmid maintenance, but may also contributes to the distribution of small antibiotic resistance plasmids among Gram-positive bacteria. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Relaxases are metal-dependent nucleases that break and join DNA for the initiation and completion of conjugative bacterial gene transfer. Conjugation is the main process through which antibiotic resistance spreads among bacteria, with multidrug-resistant staphylococci and streptococci infections posing major threats to human health. The MOBV family of relaxases accounts for approximately 85% of all relaxases found in Staphylococcus aureus isolates. Here, we present six structures of the MOBV relaxase MobM from the promiscuous plasmid pMV158 in complex with several origin of transfer DNA fragments. A combined structural, biochemical, and computational approach reveals that MobM follows a previously uncharacterized histidine/metal-dependent DNA processing mechanism, which involves the formation of a covalent phosphoramidate histidine-DNA adduct for cell-to-cell transfer. We discuss how the chemical features of the high-energy phosphorus-nitrogen bond shape the dominant position of MOBV histidine relaxases among small promiscuous plasmids and their preference toward Gram-positive bacteria. | ||
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| - | Structural basis of a histidine-DNA nicking/joining mechanism for gene transfer and promiscuous spread of antibiotic resistance.,Pluta R, Boer DR, Lorenzo-Diaz F, Russi S, Gomez H, Fernandez-Lopez C, Perez-Luque R, Orozco M, Espinosa M, Coll M Proc Natl Acad Sci U S A. 2017 Aug 8;114(32):E6526-E6535. doi:, 10.1073/pnas.1702971114. Epub 2017 Jul 24. PMID:28739894<ref>PMID:28739894</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4lvk" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
MobM Relaxase Domain (MOBV; Mob_Pre) bound to plasmid pMV158 oriT DNA (22nt+3'Phosphate). Mn-bound crystal structure at pH 4.6
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