2b4t: Difference between revisions

Revision as of 17:34, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

2B4T is a Single protein structure of sequence from Plasmodium falciparum with and as ligands. Active as Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum at 2.25 A resolution reveals intriguing extra electron density in the active site., Robien MA, Bosch J, Buckner FS, Van Voorhis WC, Worthey EA, Myler P, Mehlin C, Boni EE, Kalyuzhniy O, Anderson L, Lauricella A, Gulde S, Luft JR, DeTitta G, Caruthers JM, Hodgson KO, Soltis M, Zucker F, Verlinde CL, Merritt EA, Schoenfeld LW, Hol WG, Proteins. 2006 Mar 15;62(3):570-7. PMID:16345073

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: Single protein]]
 [[Category: Bosch, J.]]
-[[Category: Hol, W.G.J.]]
+[[Category: Hol, W G.J.]]
-[[Category: Robien, M.A.]]
+[[Category: Robien, M A.]]
-[[Category: SGPP, Structural.Genomics.of.Pathogenic.Protozoa.Consortium.]]
+[[Category: SGPP, Structural Genomics of Pathogenic Protozoa Consortium.]]
 [[Category: AES]]
 [[Category: NAD]]
@@ Line 28: / Line 28: @@
 [[Category: structural genomics of pathogenic protozoa consortium]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:16:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:09 2008''