2abw
From Proteopedia
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|PDB= 2abw |SIZE=350|CAPTION= <scene name='initialview01'>2abw</scene>, resolution 1.620Å | |PDB= 2abw |SIZE=350|CAPTION= <scene name='initialview01'>2abw</scene>, resolution 1.620Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PG4:TETRAETHYLENE GLYCOL'>PG4</scene> | + | |LIGAND= <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Pdx2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 Plasmodium falciparum]) | |GENE= Pdx2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 Plasmodium falciparum]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1r9g|1R9G]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2abw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2abw OCA], [http://www.ebi.ac.uk/pdbsum/2abw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2abw RCSB]</span> | ||
}} | }} | ||
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[[Category: Sinning, I.]] | [[Category: Sinning, I.]] | ||
[[Category: Tews, I.]] | [[Category: Tews, I.]] | ||
| - | [[Category: PG4]] | ||
[[Category: glutaminase]] | [[Category: glutaminase]] | ||
[[Category: malaria]] | [[Category: malaria]] | ||
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[[Category: vitamin b6]] | [[Category: vitamin b6]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:50:34 2008'' |
Revision as of 22:50, 30 March 2008
| |||||||
| , resolution 1.620Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Pdx2 (Plasmodium falciparum) | ||||||
| Related: | 1R9G
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Glutaminase subunit of the plasmodial PLP synthase (Vitamin B6 biosynthesis)
Overview
Vitamin B6 is one of nature's most versatile cofactors. Most organisms synthesize vitamin B6 via a recently discovered pathway employing the proteins Pdx1 and Pdx2. Here we present an in-depth characterization of the respective orthologs from the malaria parasite, Plasmodium falciparum. Expression profiling of Pdx1 and -2 shows that blood-stage parasites indeed possess a functional vitamin B6 de novo biosynthesis. Recombinant Pdx1 and Pdx2 form a complex that functions as a glutamine amidotransferase with Pdx2 as the glutaminase and Pdx1 as pyridoxal-5 '-phosphate synthase domain. Complex formation is required for catalytic activity of either domain. Pdx1 forms a chimeric bi-enzyme with the bacterial YaaE, a Pdx2 ortholog, both in vivo and in vitro, although this chimera does not attain full catalytic activity, emphasizing that species-specific structural features govern the interaction between the protein partners of the PLP synthase complexes in different organisms. To gain insight into the activation mechanism of the parasite bi-enzyme complex, the three-dimensional structure of Pdx2 was determined at 1.62 A. The obstruction of the oxyanion hole indicates that Pdx2 is in a resting state and that activation occurs upon Pdx1-Pdx2 complex formation.
About this Structure
2ABW is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.
Reference
Vitamin B6 biosynthesis by the malaria parasite Plasmodium falciparum: biochemical and structural insights., Gengenbacher M, Fitzpatrick TB, Raschle T, Flicker K, Sinning I, Muller S, Macheroux P, Tews I, Kappes B, J Biol Chem. 2006 Feb 10;281(6):3633-41. Epub 2005 Dec 8. PMID:16339145
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