3C4U
Structure of class II fructose-biphosphate aldolase from helicobacter pylori
Summary for 3C4U
Entry DOI | 10.2210/pdb3c4u/pdb |
Related | 3C52 3C56 |
Descriptor | Fructose-bisphosphate aldolase, SODIUM ION, ZINC ION, ... (4 entities in total) |
Functional Keywords | fbp aldolase, class ii, zinc, glycolysis, lyase, metal-binding |
Biological source | Helicobacter pylori (Campylobacter pylori) |
Total number of polymer chains | 2 |
Total formula weight | 67778.42 |
Authors | Coincon, M.,Sygusch, J. (deposition date: 2008-01-30, release date: 2008-08-26, Last modification date: 2023-08-30) |
Primary citation | Fonvielle, M.,Coincon, M.,Daher, R.,Desbenoit, N.,Kosieradzka, K.,Barilone, N.,Gicquel, B.,Sygusch, J.,Jackson, M.,Therisod, M. Synthesis and Biochemical Evaluation of Selective Inhibitors of Class II Fructose Bisphosphate Aldolases: Towards New Synthetic Antibiotics. Chemistry, 14:8521-8529, 2008 Cited by PubMed Abstract: We report the synthesis and biochemical evaluation of selective inhibitors of class II (zinc-dependent) fructose bisphosphate aldolases. The most active compound is a simplified analogue of fructose bisphosphate, bearing a well-positioned metal chelating group. It is a powerful and highly selective competitive inhibitor of isolated class II aldolases. We report crystallographic studies of this inhibitor bound in the active site of the Helicobacter pylori enzyme. The compound also shows activity against Mycobacterium tuberculosis isolates. PubMed: 18688832DOI: 10.1002/chem.200800857 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
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