2.1 Â structure of serratia endonuclease suggests a mechanism for binding to doublestranded dna

Mitchell D. Miller, Jack Tanner, Mary Alpaugh, Michael J. Benedik, Kurt L. Krause

Research output: Contribution to journalArticlepeer-review

100 Scopus citations

Abstract

The crystal structure of Serratia endonuclease has been solved to 2.1 Â by multiple isomorphous replacement. This magnesium-dependent enzyme is equally active against single-and double-stranded DNA, as well as RNA, without any apparent base preference. The Serratia endonuclease fold is distinct from that of other nucleases that have been solved by X-ray diffraction. The refined structure consists of a central layer containing six antiparallel ß-strands which is flanked on one side by a helical domain and on the opposite side by one dominant helix and a very long coiled loop. Electrostatic calculations reveal a strongly polarized molecular surface and suggest that a cleft between this long helix and loop, near His 89, may contain the active site of the enzyme.

Original languageEnglish (US)
Pages (from-to)461-468
Number of pages8
JournalNature Structural Biology
Volume1
Issue number7
DOIs
StatePublished - Jul 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Genetics

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