Structure of free BglII reveals an unprecedented scissor-like motion for opening an endonuclease

Christine M. Lukacs, Rebecca Kucera, Ira Schildkraut, Aneel K. Aggarwal

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Restriction endonuclease BglII completely encircles its target DNA, making contacts 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 understand how this occurs, we have solved the structure of the free enzyme at 2.3 Å resolution, as a complement to our earlier work on the BglII-DNA complex. Unexpectedly, the enzyme opens by a dramatic 'scissor-like' motion, accompanied by a complete rearrangement of the α-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. Such an 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.

Original languageEnglish
Pages (from-to)126-130
Number of pages5
JournalNature Structural Biology
Volume8
Issue number2
DOIs
StatePublished - 2001

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