1TQX

Crystal Structure of Pfal009167 A Putative D-Ribulose 5-Phosphate 3-Epimerase from P.falciparum

Summary for 1TQX

• Entry DOI: 10.2210/pdb1tqx/pdb
• Descriptor: D-ribulose-5-phosphate 3-epimerase, putative, SULFATE ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: structural genomics, protein structure initiative, psi, structural genomics of pathogenic protozoa consortium, sgpp, tim barrel, ribulose phosphate epimerase, unknown function
• Biological source: Plasmodium falciparum
• Total number of polymer chains: 2
• Total formula weight: 51476.13

Authors

Caruthers, J.,Bosch, J.,Hol, W.G.J.,Structural Genomics of Pathogenic Protozoa Consortium (SGPP) (deposition date: 2004-06-18, release date: 2004-12-21, Last modification date: 2023-08-23)

Primary citation

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.
Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum.
Proteins, 62:338-342, 2006

PubMed Abstract: 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.

PubMed: 16304640
DOI: 10.1002/prot.20764

Experimental method

X-RAY DIFFRACTION (2 Å)