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 language | English (US) |
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Pages (from-to) | 461-468 |
Number of pages | 8 |
Journal | Nature Structural Biology |
Volume | 1 |
Issue number | 7 |
DOIs | |
State | Published - Jul 1994 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Structural Biology
- Biochemistry
- Genetics