Structural highlights
Function
[NUC_STAAU] Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The x-ray crystal structure of a mutant of staphylococcal nuclease that contains a single glycine residue inserted in the C-terminal alpha-helix has been solved to 1.67 A resolution and refined to a crystallographic R value of 0.170. This inserted glycine residue is accommodated in the alpha-helix by formation of a previously uncharacterized bulge, which we term the alpha aneurism. A conformational search of known protein structures has identified the alpha aneurism in a number of protein families, including the histocompatibility antigens and hemoglobins.
The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease.,Keefe LJ, Sondek J, Shortle D, Lattman EE Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3275-9. PMID:8475069[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Keefe LJ, Sondek J, Shortle D, Lattman EE. The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3275-9. PMID:8475069
