2P1E
Crystal structure of the Leishmania infantum glyoxalase II with D-Lactate at the active site
Summary for 2P1E
| Entry DOI | 10.2210/pdb2p1e/pdb |
| Related | 2P18 |
| Descriptor | Glyoxalase II, ZINC ION, SPERMIDINE, ... (5 entities in total) |
| Functional Keywords | beta sandwich, product, spermidine, hydrolase |
| Biological source | Leishmania infantum |
| Total number of polymer chains | 1 |
| Total formula weight | 34788.84 |
| Authors | Trincao, J.,Barata, L.,Najmudin, S.,Bonifacio, C.,Romao, M.J. (deposition date: 2007-03-05, release date: 2008-01-15, Last modification date: 2023-11-15) |
| Primary citation | Silva, M.S.,Barata, L.,Ferreira, A.E.,Romao, S.,Tomas, A.M.,Freire, A.P.,Cordeiro, C. Catalysis and Structural Properties of Leishmania infantum Glyoxalase II: Trypanothione Specificity and Phylogeny. Biochemistry, 47:195-204, 2008 Cited by PubMed Abstract: The glyoxalase pathway catalyzes the formation of d-lactate from methylglyoxal, a toxic byproduct of glycolysis. In trypanosomatids, trypanothione replaces glutathione in this pathway, making it a potential drug target, since its selective inhibition might increase methylglyoxal concentration in the parasites. Two glyoxalase II structures were solved. One with a bound spermidine molecule (1.8 A) and the other with d-lactate at the active site (1.9 A). The second structure was obtained by crystal soaking with the enzyme substrate (S)-d-lactoyltrypanothione. The overall structure of Leishmania infantum glyoxalase II is very similar to its human counterpart, with important differences at the substrate binding site. The crystal structure of L. infantum glyoxalase II is the first structure of this enzyme from trypanosomatids. The differential specificity of glyoxalase II toward glutathione and trypanothione moieties was revealed by differential substrate binding. Evolutionary analysis shows that trypanosomatid glyoxalases II diverged early from eukaryotic enzymes, being unrelated to prokaryotic proteins. PubMed: 18052346DOI: 10.1021/bi700989m PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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