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

Journal article

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.

Authors: Ariza, A; Vickers, T; Greig, N; Fairlamb, A; Bond, C

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: International Union of Crystallography
• Journal: Acta Crystallographica Section F: Structural Biology Communications
• Issue: Pt 8
• Publication date: 2005-08-01
• Acceptance date: 2005-06-06
• DOI: 10.1107/S174430910502169X
• ISSN: 1744-3091
• Language: English
• Keywords: Lactoylglutathione Lyase; Models, Molecular; Leishmania major; X-Ray Diffraction; Journal Article; Animals; Crystallization; SBTMR; Research Support, Non-U.S. Gov't