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PMID: 8145855 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Structure of restriction endonuclease BamHI and its relationship to EcoRI.

Nature ·Vol. 368 ·No. 6472 ·1994-04-14 ·Pages 660-4

Newman M, Strzelecka T, Dorner LF, Schildkraut I, Aggarwal AK

Abstract

Type II restriction endonucleases are characterized by the remarkable specificity with which they cleave specific DNA sequences. Surprisingly, their protein sequences are in most cases unrelated, and no recurring structural motif has yet been identified. We have determined the structure of restriction endonuclease BamHI at 1.95 A resolution. BamHI shows striking resemblance to the structure of endonuclease EcoRI (refs 3, 4), despite the lack of sequence similarity between them. We also observe some curious differences between the two structures, and propose an evolutionary scheme that may explain them. The active site of BamHI is structurally similar to the active sites of EcoRI and EcoRV (ref. 5), but the mechanism by which BamHI activates a water molecule for nucleophilic attack may be different.

MeSH Terms
Binding Sites Biological Evolution Deoxyribonuclease BamHI/chemistry Deoxyribonuclease EcoRI/chemistry Models, Molecular Protein Structure, Secondary Protein Structure, Tertiary Structure-Activity Relationship
Chemicals
Deoxyribonuclease BamHI Deoxyribonuclease EcoRI
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Newman M
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
Strzelecka T
Dorner L F
Schildkraut I
Aggarwal A K
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1994-04-14
Pages
660-4
Language
English
Region
England
NLM ID
0410462
Subset
IM
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