1STY

THE ALPHA ANEURISM: A STRUCTURAL MOTIF REVEALED IN AN INSERTION MUTANT OF STAPHYLOCOCCAL NUCLEASE

Summary for 1STY

Entry DOI	10.2210/pdb1sty/pdb
Descriptor	STAPHYLOCOCCAL NUCLEASE, CALCIUM ION, THYMIDINE-3',5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywords	hydrolase (phosphoric diester)
Biological source	Staphylococcus aureus
Total number of polymer chains	1
Total formula weight	17342.65
Authors	Keefe, L.J.,Lattman, E.E. (deposition date: 1993-02-18, release date: 1993-04-15, Last modification date: 2024-02-14)
Primary citation	Keefe, L.J.,Sondek, J.,Shortle, D.,Lattman, E.E. The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease. Proc.Natl.Acad.Sci.USA, 90:3275-3279, 1993 Cited by PubMed Abstract: 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. PubMed: 8475069 DOI: 10.1073/pnas.90.8.3275 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.67 Å)

Structure validation