1EJB

LUMAZINE SYNTHASE FROM SACCHAROMYCES CEREVISIAE

Summary for 1EJB

• Entry DOI: 10.2210/pdb1ejb/pdb
• Related: 1C2Y 1C41 1DI0 1RVV
• Descriptor: LUMAZINE SYNTHASE, 5-(6-D-RIBITYLAMINO-2,4-DIHYDROXYPYRIMIDIN-5-YL)-1-PENTYL-PHOSPHONIC ACID (3 entities in total)
• Functional Keywords: lumazine synthase, saccharomyces cerevisiae, x-ray structure analysis, inhibitor complex, vitamin biosynthesis, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Mitochondrion intermembrane space : P50861
• Total number of polymer chains: 5
• Total formula weight: 94298.30

Authors

Meining, W.,Mortl, S.,Fischer, M.,Cushman, M.,Bacher, A.,Ladenstein, R. (deposition date: 2000-03-02, release date: 2001-03-02, Last modification date: 2024-02-07)

Primary citation

Meining, W.,Mortl, S.,Fischer, M.,Cushman, M.,Bacher, A.,Ladenstein, R.
The atomic structure of pentameric lumazine synthase from Saccharomyces cerevisiae at 1.85 A resolution reveals the binding mode of a phosphonate intermediate analogue.
J.Mol.Biol., 299:181-197, 2000

PubMed Abstract: 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 A x 82.9 A x 300.2 A. X-ray diffraction data collected under cryogenic conditions were complete to 1.85 A resolution. The structure of the enzyme in complex with the intermediate analogue, 5-(6-D-ribitylamino-2,4-dihydroxypyrimidine-5-yl)-1-pentyl-p hosphonic acid was solved via molecular replacement using the structure of the Bacillus subtilis enzyme as search model and was refined to a final R-factor of 19.8% (Rfree: 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.

PubMed: 10860731
DOI: 10.1006/jmbi.2000.3742

Experimental method

X-RAY DIFFRACTION (1.85 Å)