1f2j

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CRYSTAL STRUCTURE ANALYSIS OF ALDOLASE FROM T. BRUCEICRYSTAL STRUCTURE ANALYSIS OF ALDOLASE FROM T. BRUCEI

Structural highlights

1f2j is a 1 chain structure with sequence from Trypanosoma brucei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALF_TRYBB

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases.,Chudzik DM, Michels PA, de Walque S, Hol WG J Mol Biol. 2000 Jul 21;300(4):697-707. PMID:10891264[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Chudzik DM, Michels PA, de Walque S, Hol WG. Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases. J Mol Biol. 2000 Jul 21;300(4):697-707. PMID:10891264 doi:10.1006/jmbi.2000.3910

1f2j, resolution 1.90Å

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OCA