Full description
Rotary ATPases couple ATP hydrolysis/synthesis with proton translocation across biological membranes and so are central components of the biological energy conversion machinery. Their peripheral stalks are essential components that counteract torque generated by rotation of the central stalk during ATP synthesis or hydrolysis.
These datasets are derivatives of the peripheral stalk from T.thermophilus A-ATPase. Native crystals were soaked in Lutetium(III) acetate (2K7c_3_###.img) and Dysprosium(III) chloride (2K3#######.img).
Resulting maps were used to create the pdb model 3V6I. The model was used to identify bending and twisting motions inherent within the structure that accommodate movements within the ATPase.
- Beamline: MX2
- EPN: 3511
- PDB: 3V61
- Organism: Thermus thermophilus HB8
- Expression System: Escherichia coli
- Sequence: >3V6I:B|PDBID|CHAIN|SEQUENCE GMGGLGLIKSLAEKEKQLLERLEAAKKEAEERVKRAEAEAKALLEEAEAKAKALEAQYRERERAETEALLARYRERAEAE AKAVREKAMARLDEAVALVLKEVLP
Available: 24 03 2014
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