The atomic structure of pentameric lumazine synthase from Saccharomyces cerevisiae at 1.85 angstrom resolution reveals the binding mode of a phosphonate intermediate analogue
2000 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 299, no 1, 181-197 p.Article in journal (Refereed) Published
Lumazine synthase of Saccharomyces cerevisiae is a homopentamer with a molecular weight of 90 kDa. Crystals of the recombinant enzyme with a size of up to 1.6 mm were obtained. The space group is P4(1)2(1)2 with lattice dimensions 82.9 Angstrom * 82.9 Angstrom * 300.2 Angstrom. X-ray diffraction data collected under cryogenic conditions were complete to 1.85 Angstrom resolution. The structure of the enzyme in complex with the intermediate analogue, 5-(6-D-ribitylamino-2,4-dihydroxypyrimidine-5-yl)-1-pentyl-phosphonic acid was solved via molecular replacement using the structure of the Bacillus subtilis enzyme as search model and was refined to a final X-factor of 19.8% (R-free:22.5%). The conformation of the active site ligand of the enzyme mimicks that of the Schiff base intermediate of the enzyme-catalyzed reaction. The data enable the reconstruction of the reactant topology during the early steps of the catalytic reaction. Structural determinants, which are likely to be responsible for the inability of the S. cerevisiae enzyme to form icosahedral capsids, will be discussed.
Place, publisher, year, edition, pages
2000. Vol. 299, no 1, 181-197 p.
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:sh:diva-15750DOI: 10.1006/jmbi.2000.3742ISI: 000087289400013PubMedID: 10860731ScopusID: 2-s2.0-0034716938OAI: oai:DiVA.org:sh-15750DiVA: diva2:508082