1EPX
CRYSTAL STRUCTURE ANALYSIS OF ALDOLASE FROM L. MEXICANA
Summary for 1EPX
| Entry DOI | 10.2210/pdb1epx/pdb |
| Descriptor | FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE (2 entities in total) |
| Functional Keywords | beta barrel, pts signal, aldolase, leishmania, fructose-1, 6-bisphosphate, lyase |
| Biological source | Leishmania mexicana |
| Total number of polymer chains | 4 |
| Total formula weight | 162894.16 |
| Authors | Chudzik, D.M.,Michels, P.A.,de Walque, S.,Hol, W.G.J. (deposition date: 2000-03-29, release date: 2000-07-13, Last modification date: 2024-04-03) |
| Primary citation | Chudzik, D.M.,Michels, P.A.,de Walque, S.,Hol, W.G. Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases. J.Mol.Biol., 300:697-707, 2000 Cited by PubMed Abstract: Trypanosomatids, unicellular organisms responsible for several global diseases, contain unique organelles called glycosomes in which the first seven glycolytic enzymes are sequestered. We report the crystal structures of glycosomal fructose-1,6-bisphosphate aldolase from two major tropical pathogens, Trypanosoma brucei and Leishmania mexicana, the causative agents of African sleeping sickness and one form of leishmaniasis, respectively. Unlike mammalian aldolases, the T. brucei and L. mexicana aldolases contain nonameric N-terminal type 2 peroxisomal targeting signals (PTS2s) to direct their import into the glycosome. In both tetrameric trypanosomatid aldolases, the PTS2s from two different subunits form two closely intertwined structures. These "PTS2 dimers", which have very similar conformations in the two aldolase structures, are the first reported conformations of a glycosomal or peroxisomal PTS2, and provide opportunities for the design of trypanocidal compounds. PubMed: 10891264DOI: 10.1006/jmbi.2000.3910 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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