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4BE7

MUTANT (K220R) OF THE HSDR SUBUNIT OF THE ECOR124I RESTRICTION ENZYME IN COMPLEX WITH ATP

Replaces:  2W74
Summary for 4BE7
Entry DOI10.2210/pdb4be7/pdb
DescriptorTYPE I RESTRICTION ENZYME ECOR124II R PROTEIN, ADENOSINE-5'-TRIPHOSPHATE, PHOSPHATE ION, ... (5 entities in total)
Functional Keywordshydrolase, dna restriction, dna modification
Biological sourceESCHERICHIA COLI
Total number of polymer chains2
Total formula weight242056.61
Authors
Csefalvay, E.,Lapkouski, M.,Guzanova, A.,Csefalvay, L.,Baikova, T.,Shevelev, I.,Janscak, P.,Smatanova, I.K.,Panjikar, S.,Carey, J.,Weiserova, M.,Ettrich, R. (deposition date: 2013-03-06, release date: 2014-03-26, Last modification date: 2023-12-20)
Primary citationCsefalvay, E.,Lapkouski, M.,Guzanova, A.,Csefalvay, L.,Baikova, T.,Shevelev, I.,Bialevich, V.,Shamayeva, K.,Janscak, P.,Kuta Smatanova, I.,Panjikar, S.,Carey, J.,Weiserova, M.,Ettrich, R.
Functional Coupling of Duplex Translocation to DNA Cleavage in a Type I Restriction Enzyme.
Plos One, 10:28700-, 2015
Cited by
PubMed Abstract: Type I restriction-modification enzymes are multifunctional heteromeric complexes with DNA cleavage and ATP-dependent DNA translocation activities located on motor subunit HsdR. Functional coupling of DNA cleavage and translocation is a hallmark of the Type I restriction systems that is consistent with their proposed role in horizontal gene transfer. DNA cleavage occurs at nonspecific sites distant from the cognate recognition sequence, apparently triggered by stalled translocation. The X-ray crystal structure of the complete HsdR subunit from E. coli plasmid R124 suggested that the triggering mechanism involves interdomain contacts mediated by ATP. In the present work, in vivo and in vitro activity assays and crystal structures of three mutants of EcoR124I HsdR designed to probe this mechanism are reported. The results indicate that interdomain engagement via ATP is indeed responsible for signal transmission between the endonuclease and helicase domains of the motor subunit. A previously identified sequence motif that is shared by the RecB nucleases and some Type I endonucleases is implicated in signaling.
PubMed: 26039067
DOI: 10.1371/JOURNAL.PONE.0128700
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.744 Å)
Structure validation

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