Literature DB >> 8475069

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

L J Keefe1, J Sondek, D Shortle, E E Lattman.   

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.

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Year:  1993        PMID： 8475069      PMCID： PMC46282          DOI： 10.1073/pnas.90.8.3275

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  15 in total

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Authors:  J Sondek; D Shortle
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Review 3.  Staphylococcal nuclease reviewed: a prototypic study in contemporary enzymology. IV. The nuclease as a model for protein folding.

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Review 5.  Staphylococcal nuclease reviewed: a prototypic study in contemporary enzymology. I. Isolation; physical and enzymatic properties.

Authors:  P W Tucker; E E Hazen; F A Cotton
Journal:  Mol Cell Biochem       Date:  1978-12-22       Impact factor: 3.396

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Authors:  A E Eriksson; W A Baase; X J Zhang; D W Heinz; M Blaber; E P Baldwin; B W Matthews
Journal:  Science       Date:  1992-01-10       Impact factor: 47.728

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Authors:  J Sondek; D Shortle
Journal:  Proc Natl Acad Sci U S A       Date:  1992-04-15       Impact factor: 11.205
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  22 in total

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9.  Side-chain entropy and packing in proteins.

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10.  Solution structures of staphylococcal nuclease from multidimensional, multinuclear NMR: nuclease-H124L and its ternary complex with Ca2+ and thymidine-3',5'-bisphosphate.

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