Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum

被引：16

作者：

Caruthers, J

Bosch, J

Buckner, F

Van Voorhis, W

Myler, P

Worthey, E

Mehlin, C

Boni, E

DeTitta, G

Luft, J

Lauricella, A

Kalyuzhniy, O

Anderson, L

Zucker, F

Soltis, M

Hol, WGJ

机构：

[1] Univ Washington, Dept Biochem, Seattle, WA 98195 USA

[2] Univ Washington, Div Infect Dis, Seattle, WA 98195 USA

[3] Univ Washington, Howard Hughes Med Inst, Seattle, WA 98195 USA

[4] Hauptman Woodward Inst, Buffalo, NY USA

[5] Seattle Biomed Res Inst, Seattle, WA 98109 USA

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2006年 / 62卷 / 02期

关键词：

malaria; shikimate; heme detoxification;

D O I：

10.1002/prot.20764

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of Pfa1009167AAA, a putative ribulose 5-phosphate 3-epimerase (PfalRPE) from Plasmodium falciparum, has been determined to 2 A resolution. RPE represents an exciting potential drug target for developing antimalarials because it is involved in the shikimate and the pentose phosphate pathways. The structure is a classic TIM-barrel fold. A coordinated Zn ion and a bound sulfate ion in the active site of the enzyme allow for a greater understanding of the mechanism of action of this enzyme. This structure is solved in the framework of the Structural Genomics of Pathogenic Protozoa (SGPP) consortium.

引用

页码：338 / 342

页数：5

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