Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum.
The crystal structure of Pfal009167AAA, 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.
Caruthers
J
J
SLAC, Stanford University, Menlo Park, California, USA.
Bosch
J
J
Buckner
F
F
Van Voorhis
W
W
Myler
P
P
Worthey
E
E
Mehlin
C
C
Boni
E
E
DeTitta
G
G
Luft
J
J
Lauricella
A
A
Kalyuzhniy
O
O
Anderson
L
L
Zucker
F
F
Soltis
M
M
Hol
Wim G J
WG
D000818:Animals; D000962:Antimalarials / Q000138:chemical synthesis; D001665:Binding Sites; D002238:Carbohydrate Epimerases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D015195:Drug Design; D008958:Models, Molecular; D010963:Plasmodium falciparum / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D017510:Protein Folding; D017433:Protein Structure, Secondary; D015800:Protozoan Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D012542:Scattering, Radiation; D013499:Surface Properties; D014961:X-Ray Diffraction / Q000379:methods
D000962:Antimalarials; D015800:Protozoan Proteins; D011994:Recombinant Proteins; D002238:Carbohydrate Epimerases; C022553:ribulosephosphate 3-epimerase