Crystallization and preliminary X-ray analysis of Leishmania major glyoxalase I

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Antonio ArizaCharles S Bond

Abstract

Glyoxalase I (GLO1) is a putative drug target for trypanosomatids, which are pathogenic protozoa that include the causative agents of leishmaniasis. Significant sequence and functional differences between Leishmania major and human GLO1 suggest that it may make a suitable template for rational inhibitor design. L. major GLO1 was crystallized in two forms: the first is extremely disordered and does not diffract, while the second, an orthorhombic form, produces diffraction to 2.0 A. Molecular-replacement calculations indicate that there are three GLO1 dimers in the asymmetric unit, which take up a helical arrangement with their molecular dyads arranged approximately perpendicular to the c axis. Further analysis of these data are under way.

References

Feb 5, 1974·Journal of Molecular Biology·B W Matthews
Nov 28, 2002·Acta Crystallographica. Section D, Biological Crystallography·Thomas C Terwilliger
Oct 29, 2003·Trends in Parasitology·Alan H Fairlamb
Feb 21, 2004·The Journal of Biological Chemistry·Thorsten Irsch, R Luise Krauth-Siegel
Aug 27, 2004·Proceedings of the National Academy of Sciences of the United States of America·Tim J VickersAlan H Fairlamb
Dec 2, 2004·Acta Crystallographica. Section D, Biological Crystallography·Paul Emsley, Kevin Cowtan

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Citations

May 7, 2010·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Lídia BarataCarlos Cordeiro
Mar 22, 2014·Biochemical Society Transactions·John F Honek
Sep 9, 2006·The Biochemical Journal·Neil GreigAlan H Fairlamb
Dec 15, 2020·Inorganic Chemistry·Sonia JafariMehdi Irani

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