The α aneurism: A structural motif revealed in an insertion mutant of staphylococcal nuclease

Lisa J. Keefe, John Sondek, David R Shortle, Eaton E. Lattman

Research output: Contribution to journalArticle

Abstract

The x-ray crystal structure of a mutant of staphylococcal nuclease that contains a single glycine residue inserted in the C-terminal α-helix has been solved to 1.67 Å resolution and refined to a crystallographic R value of 0.170. This inserted glycine residue is accommodated in the α-helix by formation of a previously uncharacterized bulge, which we term the α aneurism. A conformational search of known protein structures has identified the α aneurism in a number of protein families, including the histocompatibility antigens and hemoglobins.

Original languageEnglish (US)
Pages (from-to)3275-3279
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume90
Issue number8
StatePublished - Apr 15 1993

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Micrococcal Nuclease
Glycine
Histocompatibility Antigens
Hemoglobins
Proteins
X-Rays

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

The α aneurism : A structural motif revealed in an insertion mutant of staphylococcal nuclease. / Keefe, Lisa J.; Sondek, John; Shortle, David R; Lattman, Eaton E.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 90, No. 8, 15.04.1993, p. 3275-3279.

Research output: Contribution to journalArticle

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