1DQU

CRYSTAL STRUCTURE OF THE ISOCITRATE LYASE FROM ASPERGILLUS NIDULANS

Summary for 1DQU

• Entry DOI: 10.2210/pdb1dqu/pdb
• Descriptor: ISOCITRATE LYASE (1 entity in total)
• Functional Keywords: beta barrel, lyase
• Biological source: Emericella nidulans
• Cellular location: Glyoxysome : P28298
• Total number of polymer chains: 1
• Total formula weight: 60398.34

Authors

Britton, K.L.,Langridge, S.J.,Baker, P.J.,Weeradechapon, K.,Sedelnikova, S.E.,De Lucas, J.R.,Rice, D.W.,Turner, G. (deposition date: 2000-01-05, release date: 2000-05-10, Last modification date: 2024-02-07)

Primary citation

Britton, K.,Langridge, S.,Baker, P.J.,Weeradechapon, K.,Sedelnikova, S.E.,De Lucas, J.R.,Rice, D.W.,Turner, G.
The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans.
Structure Fold.Des., 8:349-362, 2000

PubMed Abstract: Isocitrate lyase catalyses the first committed step of the carbon-conserving glyoxylate bypass, the Mg(2+)-dependent reversible cleavage of isocitrate into succinate and glyoxylate. This metabolic pathway is an inviting target for the control of a number of diseases, because the enzymes involved in this cycle have been identified in many pathogens including Mycobacterium leprae and Leishmania.

PubMed: 10801489
DOI: 10.1016/S0969-2126(00)00117-9

Experimental method

X-RAY DIFFRACTION (2.8 Å)