3mfy

Structural characterization of the subunit A mutant F236A of the A-ATP synthase from Pyrococcus horikoshii

PDB structure
Accession
3mfy
Experiment typeX-ray
Resolution2.35 Å
ChainsA
Released7 July 2010

Chain A ( O57728)

Domains in the chain
158850100150200250300350400450500550
200400
PDB: Chain A
ATP-synt_V…V_A-ATPase_AATP-synt_V_A-type_…
Representative domains
ATP-synt_V_A-type_alpha_N
V_A-ATPase_A
ATP-synt_V_A-type_alpha_C

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

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.