5E9F
Structural insights of isocitrate lyases from Magnaporthe oryzae
Summary for 5E9F
| Entry DOI | 10.2210/pdb5e9f/pdb |
| Related | 5E9G 5E9H |
| Descriptor | Isocitrate lyase, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | tim beta/alpha-barrel, lyase activity, lyase |
| Biological source | Magnaporthe oryzae 70-15 (Rice blast fungus) |
| Total number of polymer chains | 4 |
| Total formula weight | 250656.48 |
| Authors | Park, Y.,Cho, Y.,Lee, Y.-H.,Lee, Y.-W.,Rhee, S. (deposition date: 2015-10-15, release date: 2016-04-27, Last modification date: 2023-11-08) |
| Primary citation | Park, Y.,Cho, Y.,Lee, Y.-H.,Lee, Y.-W.,Rhee, S. Crystal structure and functional analysis of isocitrate lyases from Magnaporthe oryzae and Fusarium graminearum J.Struct.Biol., 194:395-403, 2016 Cited by PubMed Abstract: The glyoxylate cycle bypasses a CO2-generating step in the tricarboxylic acid (TCA) cycle and efficiently assimilates C2 compounds into intermediates that can be used in later steps of the TCA cycle. It plays an essential role in pathogen survival during host infection such that the enzymes involved in this cycle have been suggested as potential drug targets against human pathogens. Isocitrate lyase (ICL) catalyzes the first-step reaction of the glyoxylate cycle, using isocitrate from the TCA cycle as the substrate to produce succinate and glyoxylate. In this study we report the crystal structure of Magnaporthe oryzae ICL in both the ligand-free form and as a complex with Mg(2+), glyoxylate, and glycerol, as well as the structure of the Fusarium graminearum ICL complexed with Mn(2+) and malonate. We also describe the ligand-induced conformational changes in the catalytic loop and C-terminal region, both of which are essential for catalysis. Using various mutant ICLs in an activity assay, we gained insight into the function of residues within the active site. These structural and functional analyses provide detailed information with regard to fungal ICLs. PubMed: 27016285DOI: 10.1016/j.jsb.2016.03.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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