2B4R

Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum at 2.25 Angstrom Resolution reveals intriguing extra electron density in the active site

「1ZYA」から置き換えられました

2B4R の概要

• エントリーDOI: 10.2210/pdb2b4r/pdb
• 関連するPDBエントリー: 2B4T
• 分子名称: glyceraldehyde-3-phosphate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, 4-(2-AMINOETHYL)BENZENESULFONYL FLUORIDE, ... (5 entities in total)
• 機能のキーワード: sgpp, structural genomics, psi, protein structure initiative, gapdh, glyceraldehyde-3-phosphate dehydrogenase, structural genomics of pathogenic protozoa consortium, oxidoreductase
• 由来する生物種: Plasmodium falciparum (malaria parasite P. falciparum)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 154208.84

構造登録者

Robien, M.A.,Bosch, J.,Hol, W.G.J.,Structural Genomics of Pathogenic Protozoa Consortium (SGPP) (登録日: 2005-09-26, 公開日: 2005-10-04, 最終更新日: 2023-08-23)

主引用文献

Robien, M.A.,Bosch, J.,Buckner, F.S.,Van Voorhis, W.C.,Worthey, E.A.,Myler, P.,Mehlin, C.,Boni, E.E.,Kalyuzhniy, O.,Anderson, L.,Lauricella, A.,Gulde, S.,Luft, J.R.,Detitta, G.,Caruthers, J.M.,Hodgson, K.O.,Soltis, M.,Zucker, F.,Verlinde, C.L.,Merritt, E.A.,Schoenfeld, L.W.,Hol, W.G.
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum at 2.25 A resolution reveals intriguing extra electron density in the active site
Proteins, 62:570-577, 2006

PubMed Abstract: The crystal structure of D-glyceraldehyde-3-phosphate dehydrogenase (PfGAPDH) from the major malaria parasite Plasmodium falciparum is solved at 2.25 A resolution. The structure of PfGAPDH is of interest due to the dependence of the malaria parasite in infected human erythrocytes on the glycolytic pathway for its energy generation. Recent evidence suggests that PfGAPDH may also be required for other critical activities such as apical complex formation. The cofactor NAD(+) is bound to all four subunits of the tetrameric enzyme displaying excellent electron densities. In addition, in all four subunits a completely unexpected large island of extra electron density in the active site is observed, approaching closely the nicotinamide ribose of the NAD(+). This density is most likely the protease inhibitor AEBSF, found in maps from two different crystals. This putative AEBSF molecule is positioned in a crucial location and hence our structure, with expected and unexpected ligands bound, can be of assistance in lead development and design of novel antimalarials.

PubMed: 16345073
DOI: 10.1002/prot.20801

実験手法

X-RAY DIFFRACTION (2.25 Å)