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Titolo:
Structure of free Bg/II reveals an unprecedented scissor-like motion for opening an endonuclease
Autore:
Lukacs, CM; Kucera, R; Schildkraut, I; Aggarwal, AK;
Indirizzi:
CUNY Mt Sinai Sch Med, Dept Physiol & Biophys, Struct Biol Program, New York, NY 10029 USA CUNY Mt Sinai Sch Med New York NY USA 10029 ogram, New York, NY 10029 USA New England Biolabs Inc, Beverly, MA 01915 USA New England Biolabs Inc Beverly MA USA 01915 s Inc, Beverly, MA 01915 USA
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 2, volume: 8, anno: 2001,
pagine: 126 - 130
SICI:
1072-8368(200102)8:2<126:SOFBRA>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
B P50 HOMODIMER; CRYSTAL-STRUCTURE; COGNATE DNA; RESTRICTION-ENDONUCLEASE; ANGSTROM RESOLUTION; PVUII ENDONUCLEASE; ECORV ENDONUCLEASE; RECOGNITION; CLEAVAGE; COMPLEX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Aggarwal, AK CUNY Mt Sinai Sch Med, Dept Physiol & Biophys, Struct Biol Program, 1425 Madison Ave, New York, NY 10029 USA CUNY Mt Sinai Sch Med 1425 Madison Ave New York NY USA 10029
Citazione:
C.M. Lukacs et al., "Structure of free Bg/II reveals an unprecedented scissor-like motion for opening an endonuclease", NAT ST BIOL, 8(2), 2001, pp. 126-130

Abstract

Restriction endonuclease BgIII completely encircles its target DNA, makingcontacts to both the major and minor grooves. To allow the DNA to enter and leave the binding cleft, the enzyme dimer has to rearrange. To understandhow this occurs, we have solved the structure of the free enzyme at 2.3 Angstrom resolution, as a complement to our earlier work on the BgIII-DNA complex Unexpectedly, the enzyme opens by a dramatic 'scissor-like' motion, accompanied by a complete rearrangement of the or-helices at the dimer interface. Moreover, within each monomer, a set of residues - a 'lever' - lowers or raises to alternately sequester or expose the active site residues. Suchan extreme difference in free versus complexed structures has not been reported for other restriction endonucleases, This elegant mechanism for capturing DNA may extend to other enzymes that encircle DNA.

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Documento generato il 02/07/20 alle ore 22:06:29