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The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease.


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.

SUBMITTER: Keefe LJ 

PROVIDER: S-EPMC46282 | biostudies-other | 1993 Apr

REPOSITORIES: biostudies-other

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The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease.

Keefe L J LJ   Sondek J J   Shortle D D   Lattman E E EE  

Proceedings of the National Academy of Sciences of the United States of America 19930401 8


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 famili  ...[more]

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