5E9G

Structural insights of isocitrate lyases from Magnaporthe oryzae

Summary for 5E9G

• Entry DOI: 10.2210/pdb5e9g/pdb
• Related: 5E9F 5E9H
• Descriptor: Isocitrate lyase, GLYOXYLIC ACID, GLYCEROL, ... (5 entities in total)
• Functional Keywords: tim beta/alpha-barrel, lyase activity, lyase
• Biological source: Magnaporthe oryzae 70-15 (Rice blast fungus)
• Cellular location: Glyoxysome : P0CT06
• Total number of polymer chains: 4
• Total formula weight: 251172.81

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

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: 27016285
DOI: 10.1016/j.jsb.2016.03.019

Experimental method

X-RAY DIFFRACTION (2.1 Å)