Solution of the structure of tetrameric human glucose 6-phosphate dehydrogenase by molecular replacement Journal Article
| Authors: | Au, S. W. N.; Naylor, C. E.; Gover, S.; Vandeputte-Rutten, L.; Scopes, D. A.; Mason, P. J.; Luzzatto, L.; Lam, V. M. S.; Adams, M. J. |
| Article Title: | Solution of the structure of tetrameric human glucose 6-phosphate dehydrogenase by molecular replacement |
| Abstract: | Recombinant human glucose 6-phosphate dehydrogenase (G6PD) has been crystallized and its structure solved by molecular replacement. Crystals of the natural mutant R459L grow under similar conditions in space groups P212121 and C2221 with eight or four 515-residue molecules in the asymmetric unit, respectively. A non-crystallographic 222 tetramer was found in the C2221 crystal form using a 4 Å resolution data set and a dimer of the large β + α domains of the Leuconostoc mesenteroides enzyme as a search model. This tetramer was the only successful search model for the P212121 crystal form using data to 3 Å. Crystals of the deletion mutant ΔG6PD grow in space group F222 with a monomer in the asymmetric unit; 2.5 Å resolution data have been collected. Comparison of the packing of tetramers in the three space groups suggests that the N-terminal tail of the enzyme prevents crystallization with exact 222 molecular symmetry. |
| Keywords: | protein conformation; recombinant enzyme; amino acid sequence; molecular sequence data; amino terminal sequence; base sequence; crystal structure; dimerization; crystallography, x-ray; mutagenesis, site-directed; crystallization; enzyme structure; enzyme modification; tetramer; crystallography; glucose 6 phosphate dehydrogenase; glucosephosphate dehydrogenase; humans; deletion mutagenesis; leuconostoc; leuconostoc mesenteroides |
| Journal Title: | Acta Crystallographica Section D: Biological Crystallography |
| Volume: | 55 |
| Issue: | 4 |
| ISSN: | 0907-4449 |
| Publisher: | Wiley Blackwell |
| Date Published: | 1999-04-01 |
| Start Page: | 826 |
| End Page: | 834 |
| Language: | English |
| DOI: | 10.1107/s0907444999000827 |
| PUBMED: | 10089300 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |
