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© Institut Pasteur
Cristaux de cellulase, enzyme purifiée de Clostridium thermocellum permettant la digestion de la cellulose. Image colorisée.
Publication : Acta crystallographica. Section D, Biological crystallography

Crystallographic studies of two variants of Pseudomonas aeruginosa IMPDH with impaired allosteric regulation

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section D, Biological crystallography - 25 Aug 2015

Labesse G, Alexandre T, Gelin M, Haouz A, Munier-Lehmann H

Link to Pubmed [PMID] – 26327379

Acta Crystallogr. D Biol. Crystallogr. 2015 Sep;71(Pt 9):1890-9

Inosine-5′-monophosphate dehydrogenases (IMPDHs), which are the rate-limiting enzymes in guanosine-nucleotide biosynthesis, are important therapeutic targets. Despite in-depth functional and structural characterizations of various IMPDHs, the role of the Bateman domain containing two CBS motifs remains controversial. Their involvement in the allosteric regulation of Pseudomonas aeruginosa IMPDH by Mg-ATP has recently been reported. To better understand the function of IMPDH and the importance of the CBS motifs, the structure of a variant devoid of these modules (ΔCBS) was solved at high resolution in the apo form and in complex with IMP. In addition, a single amino-acid substitution variant, D199N, was also structurally characterized: the mutation corresponds to the autosomal dominant mutant D226N of human IMPDH1, which is responsible for the onset of the retinopathy adRP10. These new structures shed light onto the possible mechanism of regulation of the IMPDH enzymatic activity. In particular, three conserved loops seem to be key players in this regulation as they connect the tetramer-tetramer interface with the active site and show significant modification upon substrate binding.

http://www.ncbi.nlm.nih.gov/pubmed/26327379