Making the most of metal ions

N. C. Horton; J. J. Perona

doi:10.1038/86149

Making the most of metal ions

N. C. Horton
, J. J. Perona

Research output: Contribution to journal › Short survey › peer-review

46 Scopus citations

Abstract

Crystal structures of the homing endonuclease I-CreI bound to substrate DNA and divalent metals show that one metal ion is shared between the two active sites of the enzyme. This arrangement appears uniquely suited to the formation of double-stranded DNA breaks via a concerted reaction.

Original language	English (US)
Pages (from-to)	290-293
Number of pages	4
Journal	Nature Structural Biology
Volume	8
Issue number	4
DOIs	https://doi.org/10.1038/86149
State	Published - 2001
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

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10.1038/86149

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@article{63f1dd7adbb4412eb36d1057685ad922,

title = "Making the most of metal ions",

abstract = "Crystal structures of the homing endonuclease I-CreI bound to substrate DNA and divalent metals show that one metal ion is shared between the two active sites of the enzyme. This arrangement appears uniquely suited to the formation of double-stranded DNA breaks via a concerted reaction.",

author = "Horton, \{N. C.\} and Perona, \{J. J.\}",

note = "Funding Information: We are grateful to F. Gimble for valuable discussion and comments on the manuscript. Work in our laboratory in this area of research is funded by the National Institutes of Health and by the National Science Foundation POWRE program (N.C.H.).",

year = "2001",

doi = "10.1038/86149",

language = "English (US)",

volume = "8",

pages = "290--293",

journal = "Nature Structural Biology",

issn = "1072-8368",

publisher = "Nature Publishing Group",

number = "4",

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TY - JOUR

T1 - Making the most of metal ions

AU - Horton, N. C.

AU - Perona, J. J.

N1 - Funding Information: We are grateful to F. Gimble for valuable discussion and comments on the manuscript. Work in our laboratory in this area of research is funded by the National Institutes of Health and by the National Science Foundation POWRE program (N.C.H.).

PY - 2001

Y1 - 2001

N2 - Crystal structures of the homing endonuclease I-CreI bound to substrate DNA and divalent metals show that one metal ion is shared between the two active sites of the enzyme. This arrangement appears uniquely suited to the formation of double-stranded DNA breaks via a concerted reaction.

AB - Crystal structures of the homing endonuclease I-CreI bound to substrate DNA and divalent metals show that one metal ion is shared between the two active sites of the enzyme. This arrangement appears uniquely suited to the formation of double-stranded DNA breaks via a concerted reaction.

UR - https://www.scopus.com/pages/publications/0035066535

UR - https://www.scopus.com/pages/publications/0035066535#tab=citedBy

U2 - 10.1038/86149

DO - 10.1038/86149

M3 - Short survey

C2 - 11276242

AN - SCOPUS:0035066535

SN - 1072-8368

VL - 8

SP - 290

EP - 293

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 4

ER -

Making the most of metal ions

Abstract

ASJC Scopus subject areas

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