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

J. Caruthers; J. Bosch; F. Buckner; W. Van Voorhis; P. Myler; E. Worthey; C. Mehlin; E. Boni; G. DeTitta; J. Luft; A. Lauricella; O. Kalyuzhniy; L. Anderson; F. Zucker; M. Soltis; Wim G J Hol

doi:10.1002/prot.20764

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

J. Caruthers, J. Bosch, F. Buckner, W. Van Voorhis, P. Myler, E. Worthey, C. Mehlin, E. Boni, G. DeTitta, J. Luft, A. Lauricella, O. Kalyuzhniy, L. Anderson, F. Zucker, M. Soltis, Wim G J Hol

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

The crystal structure of Pfal009167AAA, a putative ribulose 5-phosphate 3-epimerase (PfalRPE) from Plasmodium falciparum, has been determined to 2 Å 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.

Original language	English (US)
Pages (from-to)	338-342
Number of pages	5
Journal	Proteins
Volume	62
Issue number	2
DOIs	https://doi.org/10.1002/prot.20764
State	Published - Feb 1 2006
Externally published	Yes

Keywords

Heme detoxification
Malaria
Shikimate

ASJC Scopus subject areas

Genetics
Structural Biology
Biochemistry

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10.1002/prot.20764

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title = "Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum",

abstract = "The crystal structure of Pfal009167AAA, a putative ribulose 5-phosphate 3-epimerase (PfalRPE) from Plasmodium falciparum, has been determined to 2 {\AA} 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.",

keywords = "Heme detoxification, Malaria, Shikimate",

author = "J. Caruthers and J. Bosch and F. Buckner and {Van Voorhis}, W. and P. Myler and E. Worthey and C. Mehlin and E. Boni and G. DeTitta and J. Luft and A. Lauricella and O. Kalyuzhniy and L. Anderson and F. Zucker and M. Soltis and Hol, {Wim G J}",

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volume = "62",

pages = "338--342",

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AU - Caruthers, J.

AU - Bosch, J.

AU - Buckner, F.

AU - Van Voorhis, W.

AU - Myler, P.

AU - Worthey, E.

AU - Mehlin, C.

AU - Boni, E.

AU - DeTitta, G.

AU - Luft, J.

AU - Lauricella, A.

AU - Kalyuzhniy, O.

AU - Anderson, L.

AU - Zucker, F.

AU - Soltis, M.

AU - Hol, Wim G J

PY - 2006/2/1

Y1 - 2006/2/1

N2 - The crystal structure of Pfal009167AAA, a putative ribulose 5-phosphate 3-epimerase (PfalRPE) from Plasmodium falciparum, has been determined to 2 Å 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.

AB - The crystal structure of Pfal009167AAA, a putative ribulose 5-phosphate 3-epimerase (PfalRPE) from Plasmodium falciparum, has been determined to 2 Å 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.

KW - Heme detoxification

KW - Malaria

KW - Shikimate

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DO - 10.1002/prot.20764

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JF - Proteins

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ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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