1AG1

MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE

Summary for 1AG1

• Entry DOI: 10.2210/pdb1ag1/pdb
• Descriptor: TRIOSEPHOSPHATE ISOMERASE, PHOSPHATE ION (3 entities in total)
• Functional Keywords: isomerase (intramolecular oxidoreductase), isomerase(intramolecular oxidoreductase)
• Biological source: Trypanosoma brucei
• Cellular location: Glycosome: P04789
• Total number of polymer chains: 2
• Total formula weight: 53826.63

Authors

Verlinde, C.L.M.J.,Hol, W.G.J. (deposition date: 1997-03-28, release date: 1997-06-16, Last modification date: 2024-05-22)

Primary citation

Verlinde, C.L.,Noble, M.E.,Kalk, K.H.,Groendijk, H.,Wierenga, R.K.,Hol, W.G.
Anion binding at the active site of trypanosomal triosephosphate isomerase. Monohydrogen phosphate does not mimic sulphate.
Eur.J.Biochem., 198:53-57, 1991

PubMed Abstract: The three-dimensional structure of triosephosphate isomerase complexed with the competitive inhibitor SO-4(2) was determined by X-ray crystallography to a resolution of 0.24 nm. A comparison with the native crystal structure, where SO-4(2) is bound, revealed five changes: (a) a 0.10-nm shift of the anion-binding site; (b) a further closing of the flexible loop of the enzyme; (c) a 'swinging in' of the side chain of the catalytic Glu, that is chi 1 changes from (+) to (-) synclinal; (d) an altered water structure; (e) a disappearance of the conformational heterogeneity at the C-terminus of strand beta 7. Some of these changes may be related to the different hydrogen-bond pattern about the two different anions. However, the distance of 0.10 nm between the sulphur and phosphorus positions is unexpected and remains intriguing.

PubMed: 2040290
DOI: 10.1111/j.1432-1033.1991.tb15985.x

Experimental method

X-RAY DIFFRACTION (2.36 Å)