Structural characterization of the subunit A mutant F236A of the A-ATP synthase from Pyrococcus horikoshii
Accession | 3mfy |
Experiment type | X-ray |
Resolution | 2.35 Å |
Chains | A |
Released | 7 July 2010 |
Chain A ( O57728)
References
1. The critical roles of residues P235 and F236 of subunit A of the motor protein A-ATP synthase in P-loop formation and nucleotide binding. Kumar, A., Manimekalai, M.S., Balakrishna, A.M., Priya, R., Biukovic, G., Jeyakanthan, J., Gruber, G. J. Mol. Biol. 401, 892-905, (2010). View articlePMID: 20615420
2. Nucleotide Binding States of Subunit A of the A-ATP Synthase and the Implication of P-Loop Switch in Evolution. Kumar, A., Manimekalai, M.S.S., Balakrishna, A.M., Jeyakanthan, J., Gerhard, G. J. Mol. Biol. (2009). View articlePMID: 19944110
3. Structure of the catalytic nucleotide-binding subunit A of A-type ATP synthase from Pyrococcus horikoshii reveals a novel domain related to the peripheral stalk. Maegawa, Y., Morita, H., Iyaguchi, D., Yao, M., Watanabe, N., Tanaka, I. Acta Crystallogr. D Biol. Crystallogr. 62, 483-488, (2006). View articlePMID: 16627940