The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1
| Autor: | Martin G. Montgomery, John V. Bason, Andrew G. W. Leslie, Graham C Robinson, John E. Walker, David M. Mueller, Ian M. Fearnley |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
natural inhibitor
Protein Conformation ATPase Immunology Saccharomyces cerevisiae Biology Crystallography X-Ray General Biochemistry Genetics and Molecular Biology 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Protein structure Catalytic Domain intermediate Animals Nucleotide Binding site Magnesium ion lcsh:QH301-705.5 030304 developmental biology chemistry.chemical_classification 0303 health sciences Binding Sites catalysis General Neuroscience Research Hydrolysis Proteins f1-atpase biology.organism_classification Adenosine Diphosphate Adenosine diphosphate Proton-Translocating ATPases Enzyme chemistry Biochemistry lcsh:Biology (General) biology.protein Cattle 030217 neurology & neurosurgery Research Article Protein Binding |
| Zdroj: | Open Biology, Vol 3, Iss 2 (2013) Open Biology |
| ISSN: | 2046-2441 |
| DOI: | 10.1098/rsob.120164 |
| Popis: | The structure of F 1 -ATPase from Saccharomyces cerevisiae inhibited by the yeast IF 1 has been determined at 2.5 Å resolution. The inhibitory region of IF 1 from residues 1 to 36 is entrapped between the C-terminal domains of the α DP - and β DP -subunits in one of the three catalytic interfaces of the enzyme. Although the structure of the inhibited complex is similar to that of the bovine-inhibited complex, there are significant differences between the structures of the inhibitors and their detailed interactions with F 1 -ATPase. However, the most significant difference is in the nucleotide occupancy of the catalytic β E -subunits. The nucleotide binding site in β E -subunit in the yeast complex contains an ADP molecule without an accompanying magnesium ion, whereas it is unoccupied in the bovine complex. Thus, the structure provides further evidence of sequential product release, with the phosphate and the magnesium ion released before the ADP molecule. |
| Databáze: | OpenAIRE |
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