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| Home > Publications database > Crystal Structure of the R-Protein of the Multisubunit ATP-Dependent Restriction Endonuclease NgoAVII |
| Home > Publications database > Crystal Structure of the R-Protein of the Multisubunit ATP-Dependent Restriction Endonuclease NgoAVII |
| Journal Article | PUBDB-2015-00004 |
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2014
Oxford Univ. Press
Oxford
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Please use a persistent id in citations: doi:10.1093/nar/gku1237
Abstract: The restriction endonuclease (REase) NgoAVII iscomposed of two proteins, R.NgoAVII and N.NgoAVII,and shares features of both Type II restriction en-zymes and Type I/III ATP-dependent restriction en-zymes (see accompanying paper Zaremba et al.,2014). Here we present crystal structures of theR.NgoAVII apo-protein and the R.NgoAVII C-terminaldomain bound to a specific DNA. R.NgoAVII is com-posed of two domains: an N-terminal nucleolytic PLDdomain; and a C-terminal B3-like DNA-binding do-main identified previously in BfiI and EcoRII REases,and in plant transcription factors. Structural compar-ison of the B3-like domains of R.NgoAVII, EcoRII, BfiIand the plant transcription factors revealed a con-served DNA-binding surface comprised of N- andC-arms that together grip the DNA. The C-arms ofR.NgoAVII, EcoRII, BfiI and plant B3 domains are sim-ilar in size, but the R.NgoAVII N-arm which makes themajority of the contacts to the target site is muchlonger. The overall structures of R.NgoAVII and BfiIare similar; however, whilst BfiI has stand-alone cat-alytic activity, R.NgoAVII requires an auxiliary cog-nate N.NgoAVII protein and ATP hydrolysis in or-der to cleave DNA at the target site. The structureswe present will help formulate future experiments toexplore the molecular mechanisms of intersubunitcrosstalk that control DNA cleavage by R.NgoAVIIand related endonucleases.
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