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

Department of Structural Biology

SLAC National Accelerator Laboratory
University of Washington
Seattle Biomedical Research Institute
Hauptman-Woodward Medical Research Institute, Inc.

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

18 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
Pages (from-to)	338-342
Number of pages	5
Journal	Proteins: Structure, Function and Genetics
Volume	62
Issue number	2
DOIs	https://doi.org/10.1002/prot.20764
State	Published - Feb 1 2006

Keywords

Heme detoxification
Malaria
Shikimate

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10.1002/prot.20764

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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, W. G. J. (2006). Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum. Proteins: Structure, Function and Genetics, 62(2), 338-342. https://doi.org/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.\}",

year = "2006",

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doi = "10.1002/prot.20764",

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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 2006, 'Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum', Proteins: Structure, Function and Genetics, vol. 62, no. 2, pp. 338-342. https://doi.org/10.1002/prot.20764

TY - JOUR

T1 - Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum

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

UR - https://www.scopus.com/pages/publications/30144441401

U2 - 10.1002/prot.20764

DO - 10.1002/prot.20764

M3 - Article

C2 - 16304640

AN - SCOPUS:30144441401

SN - 0887-3585

VL - 62

SP - 338

EP - 342

JO - Proteins: Structure, Function and Genetics

JF - Proteins: Structure, Function and Genetics

IS - 2

ER -

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

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