A-ATP Synthase

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<StructureSection load=1dm0 size='500' side='right' caption='Stx1', ([[1dm0]])' scene=''>
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<StructureSection load=3p20 size='500' side='right' caption='A-ATP synthase', ([[3p20]])' scene=''>
==Introduction==
==Introduction==
The A1Ao [[ATP synthase]] from archaea represents a class of chimeric ATPases/synthases, whose function and general structural design share characteristics both with vacuolar V1Vo ATPases and with F1Fo ATP synthases. <ref> http://www.ncbi.nlm.nih.gov/pubmed/16563431 </ref> A1A0 ATP synthase catalyzes the formation of the energy currency ATP by a membrane-embedded electrically-driven motor. The archaeon in this study, Pyrococcus horikoshii OT3 is an extreemophile residing in oceanic deep sea vents. ( )The membrane-embedded electrically-driven motor (A0) is very different in archaea with sometimes novel, exceptional subunit composition and coupling stoichiometries that may reflect the differences in energy-conserving mechanisms as well as adaptation to temperatures at or above 100 degrees C.
The A1Ao [[ATP synthase]] from archaea represents a class of chimeric ATPases/synthases, whose function and general structural design share characteristics both with vacuolar V1Vo ATPases and with F1Fo ATP synthases. <ref> http://www.ncbi.nlm.nih.gov/pubmed/16563431 </ref> A1A0 ATP synthase catalyzes the formation of the energy currency ATP by a membrane-embedded electrically-driven motor. The archaeon in this study, Pyrococcus horikoshii OT3 is an extreemophile residing in oceanic deep sea vents. ( )The membrane-embedded electrically-driven motor (A0) is very different in archaea with sometimes novel, exceptional subunit composition and coupling stoichiometries that may reflect the differences in energy-conserving mechanisms as well as adaptation to temperatures at or above 100 degrees C.

Revision as of 06:43, 16 November 2011

PDB ID 3p20

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As, Avi, and Apnp comparisons

Mutants


References

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