Transketolase from Leishmania mexicanaTransketolase from Leishmania mexicana

Structural highlights

1r9j is a 2 chain structure with sequence from Leishmania mexicana mexicana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.22Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8MPM3_LEIME

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

Transketolase has been characterized in Leishmania mexicana. A gene encoding this enzyme was identified and cloned. The gene was expressed in Escherichia coli and the protein was purified and characterized. An apparent K(m) of 2.75 mM for ribose 5-phosphate was determined. X-ray crystallography was used to determine the three-dimensional structure of the enzyme to a resolution of 2.2 A (1 A identical with 0.1 nm). The C-terminus of the protein contains a type-1 peroxisome-targeting signal, suggestive of a possible glycosomal subcellular localization. Subcellular localization experiments performed with promastigote forms of the parasite revealed that the protein was predominantly cytosolic, although a significant component of the total activity was associated with the glycosomes. Transketolase is thus the first enzyme of the nonoxidative branch of the pentose phosphate pathway whose presence has been demonstrated in a peroxisome-like organelle.

Transketolase from Leishmania mexicana has a dual subcellular localization.,Veitch NJ, Maugeri DA, Cazzulo JJ, Lindqvist Y, Barrett MP Biochem J. 2004 Sep 1;382(Pt 2):759-67. PMID:15149284[1]

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

See Also

References

  1. Veitch NJ, Maugeri DA, Cazzulo JJ, Lindqvist Y, Barrett MP. Transketolase from Leishmania mexicana has a dual subcellular localization. Biochem J. 2004 Sep 1;382(Pt 2):759-67. PMID:15149284 doi:10.1042/BJ20040459

1r9j, resolution 2.22Å

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