4BI5

CRYSTAL STRUCTURE OF A DOUBLE MUTANT (C202A AND C222D) OF TRIOSEPHOSPHATE ISOMERASE FROM GIARDIA LAMBLIA.

Replaces:  2YC8

Summary for 4BI5

• Entry DOI: 10.2210/pdb4bi5/pdb
• Related: 4BI6 4BI7
• Descriptor: TRIOSEPHOSPHATE ISOMERASE (1 entity in total)
• Functional Keywords: isomerase
• Biological source: GIARDIA INTESTINALIS
• Total number of polymer chains: 20
• Total formula weight: 553235.40

Authors

Torres-Larios, A.,Enriquez-Flores, S.,Reyes-Vivas, H.,Oria-Hernandez, J.,Hernandez-Alcantara, G. (deposition date: 2013-04-09, release date: 2013-06-05, Last modification date: 2023-12-20)

Primary citation

Hernandez-Alcantara, G.,Torres-Larios, A.,Enriquez-Flores, S.,Garcia-Torres, I.,Castillo-Villanueva, A.,Mendez, S.T.,De La Mora-De La Mora, I.,Gomez-Manzo, S.,Torres-Arroyo, A.,Lopez-Velazquez, G.,Reyes-Vivas, H.,Oria-Hernandez, J.
Structural and Functional Perturbation of Giardia Lamblia Triosephosphate Isomerase by Modification of a Non-Catalytic, Non-Conserved Region.
Plos One, 8:69031-, 2013

PubMed Abstract: We have previously proposed triosephosphate isomerase of Giardia lamblia (GlTIM) as a target for rational drug design against giardiasis, one of the most common parasitic infections in humans. Since the enzyme exists in the parasite and the host, selective inhibition is a major challenge because essential regions that could be considered molecular targets are highly conserved. Previous biochemical evidence showed that chemical modification of the non-conserved non-catalytic cysteine 222 (C222) inactivates specifically GlTIM. The inactivation correlates with the physicochemical properties of the modifying agent: addition of a non-polar, small chemical group at C222 reduces the enzyme activity by one half, whereas negatively charged, large chemical groups cause full inactivation.

PubMed: 23894402
DOI: 10.1371/JOURNAL.PONE.0069031

Experimental method

X-RAY DIFFRACTION (2.7 Å)