Structure of the catalytic domain ofPlasmodium falciparumARF GTPase-activating protein (ARFGAP)
| Autor: | Debasish Chattopadhyay, William J. Cook, Olga Senkovich |
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| Rok vydání: | 2011 |
| Předmět: |
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Molecular ADP ribosylation factor GTPase-activating protein Dimer Molecular Sequence Data Plasmodium falciparum Biophysics Sequence alignment Crystal structure Biology Biochemistry chemistry.chemical_compound Structural Biology Catalytic Domain parasitic diseases Genetics Animals Humans Structural Communications Amino Acid Sequence Peptide sequence ADP-Ribosylation Factors Condensed Matter Physics biology.organism_classification chemistry Domain (ring theory) Sequence Alignment |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:1339-1344 |
| ISSN: | 1744-3091 |
| Popis: | The crystal structure of the catalytic domain of the ADP ribosylation factor GTPase-activating protein (ARFGAP) from Plasmodium falciparum has been determined and refined to 2.4 Å resolution. Multiwavength anomalous diffraction (MAD) data were collected utilizing the Zn(2+) ion bound at the zinc-finger domain and were used to solve the structure. The overall structure of the domain is similar to those of mammalian ARFGAPs. However, several amino-acid residues in the area where GAP interacts with ARF1 differ in P. falciparum ARFGAP. Moreover, a number of residues that form the dimer interface in the crystal structure are unique in P. falciparum ARFGAP. |
| Databáze: | OpenAIRE |
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