Structural studies of Plasmodium falciparum GTP:AMP phosphotransferase
Abstract only Malaria is a global health concern accounting for approximately 219 million cases and an estimated 660 000 deaths in 2010[1]. The most fatal strain of malarial parasite, Plasmodium falciparum is found to contain 3 adenylate kinases (PfAK1, PfAK2 and PfGAK). Adenylate kinases are import...
Saved in:
| Published in: | Acta crystallographica. Section A, Foundations and advances Vol. 70; no. a1; p. C457 |
|---|---|
| Main Authors: | , |
| Format: | Journal Article |
| Language: | English |
| Published: |
05-08-2014
|
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Summary: | Abstract only Malaria is a global health concern accounting for approximately 219 million cases and an estimated 660 000 deaths in 2010[1]. The most fatal strain of malarial parasite, Plasmodium falciparum is found to contain 3 adenylate kinases (PfAK1, PfAK2 and PfGAK). Adenylate kinases are important enzymes that essentially catalyze and regulate energy metabolism processes. PfAK1 and PfAK2 catalyze the reversible MG2+ reaction ATP + AMP -> 2ADP whereas, the PfGAK catalyzes the Mg2+ dependent reaction GTP+AMP -> ADP+GDP. PfGAK was successfully cloned and expressed in Escherichia Coli. Furthermore, using 2-step chromatography the enzyme was purified and screened for crystallization conditions. PfGAK crystallized into brown hexagonal crystals and diffracted at a 2.9 Å resolution. The apo-structure have been solved and now we are working on determining the structure for PfGAK when bound to its substrate analog GP5A. |
|---|---|
| ISSN: | 2053-2733 2053-2733 |
| DOI: | 10.1107/S2053273314095424 |