4BI7

CRYSTAL STRUCTURE OF A MUTANT (C202A) OF TRIOSEPHOSPHATE ISOMERASE FROM GIARDIA LAMBLIA COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID

「2YC7」から置き換えられました

4BI7 の概要

• エントリーDOI: 10.2210/pdb4bi7/pdb
• 関連するPDBエントリー: 4BI5 4BI6
• 分子名称: TRIOSEPHOSPHATE ISOMERASE, 2-PHOSPHOGLYCOLIC ACID, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: isomerase
• 由来する生物種: GIARDIA INTESTINALIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28160.22

構造登録者

Torres-Larios, A.,Enriquez-Flores, S.,Reyes-Vivas, H.,Oria-Hernandez, J.,Hernandez-Alcantara, G. (登録日: 2013-04-09, 公開日: 2013-05-29, 最終更新日: 2024-05-01)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.6 Å)