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5n2q

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MobM Relaxase Domain (MOBV; Mob_Pre) bound to 26nt pMV158 oriT DNA

Structural highlights

5n2q is a 2 chain structure with sequence from Plasmid pMV158 and Streptococcus agalactiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

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.

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^[1]

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

References

↑ Pluta R, Boer DR, Lorenzo-Diaz F, Russi S, Gomez H, Fernandez-Lopez C, Perez-Luque R, Orozco M, Espinosa M, Coll M. Structural basis of a histidine-DNA nicking/joining mechanism for gene transfer and promiscuous spread of antibiotic resistance. 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 doi:http://dx.doi.org/10.1073/pnas.1702971114

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5n2q"

@@ Line 1: / Line 1: @@
 ==MobM Relaxase Domain (MOBV; Mob_Pre) bound to 26nt pMV158 oriT DNA==
-<StructureSection load='5n2q' size='340' side='right' caption='[[5n2q]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='5n2q' size='340' side='right'caption='[[5n2q]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5n2q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N2Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5n2q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmid_pMV158 Plasmid pMV158] and [https://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N2Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5n2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n2q OCA], [http://pdbe.org/5n2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n2q RCSB], [http://www.ebi.ac.uk/pdbsum/5n2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n2q 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=5n2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n2q OCA], [https://pdbe.org/5n2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n2q RCSB], [https://www.ebi.ac.uk/pdbsum/5n2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n2q ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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 ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Boer, D R]]
+[[Category: Large Structures]]
-[[Category: Coll, M]]
+[[Category: Plasmid pMV158]]
-[[Category: Russi, S]]
+[[Category: Streptococcus agalactiae]]
-[[Category: Conjugation]]
+[[Category: Boer DR]]
-[[Category: Dna binding protein]]
+[[Category: Coll M]]
-[[Category: Nuclease]]
+[[Category: Russi S]]
-[[Category: Relaxase]]

5n2q

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Current revision

MobM Relaxase Domain (MOBV; Mob_Pre) bound to 26nt pMV158 oriT DNA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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