Crystallographic quaternary structural analysis of AMP nucleosidases from Escherichia coli and Azotobacter vinelandii.

V. L. Giranda, H. M. Berman, Vern L. Schramm

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Adenosine monophosphate nucleosidases from Azotobacter vinelandii and Escherichia coli have been studied crystallographically to determine their quarternary structures. Preliminary characterization of the A. vinelandii enzyme shows that the crystals are monoclinic, C2 with a = 347 A, b = 204 A, c = 114 A, and beta = 91.7 degrees. The asymmetric unit contains 12 or 9 subunits of Mr 54,000. Self-rotation functions with data from the AMP nucleosidases from A. vinelandii and from E. coli (Giranda, V. L., Berman, H. M., and Schramm, V. L. (1986) J. Biol. Chem. 261, 15307-15309) are consistent with the monomers arranged as hexamers with point symmetry 32. The hexamers are arranged in the unit cells so that crystallographic 2-fold axes are coincident with the local 2-folds of the point group 32.

Original languageEnglish (US)
Pages (from-to)15674-15680
Number of pages7
JournalJournal of Biological Chemistry
Volume264
Issue number26
StatePublished - Sep 15 1989
Externally publishedYes

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AMP nucleosidase
Azotobacter vinelandii
Structural analysis
Escherichia coli
N-Glycosyl Hydrolases
adenosine nucleosidase
Point groups
Adenosine Monophosphate
Monomers
Crystals
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Crystallographic quaternary structural analysis of AMP nucleosidases from Escherichia coli and Azotobacter vinelandii. / Giranda, V. L.; Berman, H. M.; Schramm, Vern L.

In: Journal of Biological Chemistry, Vol. 264, No. 26, 15.09.1989, p. 15674-15680.

Research output: Contribution to journalArticle

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