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Biochemistry, Biophysics, and Structural Biology

Cleveland State University

Series

1999

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Full-Text Articles in Life Sciences

Three-Dimensional Structure Of The Gly121tyr Dimeric Form Of Ornithine Decarboxylase From Lactobacillus 30a, Jacqueline Vitali, Donald Carroll, Rochika G. Chaudhrya, Marvin L. Hackert Dec 1999

Three-Dimensional Structure Of The Gly121tyr Dimeric Form Of Ornithine Decarboxylase From Lactobacillus 30a, Jacqueline Vitali, Donald Carroll, Rochika G. Chaudhrya, Marvin L. Hackert

Physics Faculty Publications

Ornithine decarboxylases catalyze the conversion of ornithine to putrescine at the beginning of the polyamine pathway. Ornithine decarboxylase (ODC) from Lactobacillus 30a is a 990612 Da dodecamer composed of six homodimers. A single point mutation (Gly121Tyr) was found to prevent association of dimers into dodecamers. The dimeric protein has been crystallized at pH 7.0 in the presence of guanosine triphosphate (GTP). Crystals belong to space group P3221, with unit-cell parameters a = 111.8, c = 135.9 Å and one monomer in the asymmetric unit. The structure was determined by molecular replacement and refined using simulated annealing to …

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