TY  - JOUR
AU  - Tamulaitiene, G.
AU  - Silanskas, A.
AU  - Grazulis, S.
AU  - Zaremba, M.
AU  - Siksnys, V.
TI  - Crystal Structure of the R-Protein of the Multisubunit ATP-Dependent Restriction Endonuclease NgoAVII
JO  - Nucleic acids symposium series
VL  - 42
IS  - 22
SN  - 1362-4962
CY  - Oxford
PB  - Oxford Univ. Press
M1  - PUBDB-2015-00004
SP  - 14022 - 14030
PY  - 2014
N1  - OA
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000347916900056
C6  - pmid:25429979
DO  - DOI:10.1093/nar/gku1237
UR  - https://bib-pubdb1.desy.de/record/205427
ER  -