4LVM

MobM Relaxase Domain (MOBV; Mob_Pre) bound to plasmid pMV158 oriT DNA (23nt). Mn-bound crystal structure at pH 6.5

Summary for 4LVM

• Entry DOI: 10.2210/pdb4lvm/pdb
• Related: 4LVI 4LVJ 4LVK 4LVL
• Descriptor: Plasmid recombination enzyme, ACTTTAT oligonucleotide, ATAAAGTATAGTGTGT oligonucleotide, ... (8 entities in total)
• Functional Keywords: protein-dna complex, pfam family: mob_pre (pf01076). mob relaxase family: mobv, relaxase/endonuclease, orit dna, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Streptococcus agalactiae; More
• Total number of polymer chains: 6
• Total formula weight: 60799.62

Authors

Pluta, R.,Boer, D.R.,Coll, M. (deposition date: 2013-07-26, release date: 2014-09-24, Last modification date: 2024-02-28)

Primary citation

Pluta, R.,Boer, D.R.,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., 114:E6526-E6535, 2017

PubMed Abstract: 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 MOB family of relaxases accounts for approximately 85% of all relaxases found in isolates. Here, we present six structures of the MOB 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 MOB histidine relaxases among small promiscuous plasmids and their preference toward Gram-positive bacteria.

PubMed: 28739894
DOI: 10.1073/pnas.1702971114

Experimental method

X-RAY DIFFRACTION (3.1 Å)