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Crystallization and Phasing of Alanine Dehydrogenase From Archaeoglobus Fulgidus

Published

Author(s)

N Smith, M P. Mayhew, Hugh Robinson, A Heroux, D Charlton, Marcia J. Holden, David T. Gallagher

Abstract

Alanine dehydrogenase (AlaDH) from the hyperthermophilic archaeon A. fudgidus is a dimer of 35 kdal chains. The gene (AF1665) is annotated as an ornithine cyclodeaminase based on homology with the ornithine deaminase/ mu crystallin enzyme family. It catalyzes the NAD-dependent interconversion of alanine and pyruvate, yet shows no homology with previously known AlaDHs. We have cloned and crystallized this protein in several forms. Although the purified protein crystallizes readily under many conditions, most of the crystals diffract weakly or not at all. One polymorph growing in space group P212121 has noncrystallographic symmetry that becomes crystallographic, changing the space group to P21212, upon binding iridium or samarium. Before and after derivatization, these crystals diffract to 2.8 A using synchrotron radiation. Multiwavelength diffraction data were collected from the nonisomorphous iridium derivative, enabling structure determination
Citation
ACTA Crystallographica Section D-Biological Crystallography
Volume
59
Issue
Part 12

Keywords

Alanine dehydrogenase (AlaDH), Crystallization

Citation

Smith, N. , Mayhew, M. , Robinson, H. , Heroux, A. , Charlton, D. , Holden, M. and Gallagher, D. (2003), Crystallization and Phasing of Alanine Dehydrogenase From Archaeoglobus Fulgidus, ACTA Crystallographica Section D-Biological Crystallography (Accessed June 14, 2024)

Issues

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Created December 1, 2003, Updated February 19, 2017