Bioenergetics of archaea: ancient energy conserving mechanisms developed in the early history of life.
A key component in cellular bioenergetics is the ATP synthase. The enzyme from archaea represents a new class of ATPases, the A1AO ATP synthases. They are composed of two domains that function as a pair of rotary motors connected by a central and peripheral stalk(s). The structure of the chemically-driven motor (A1) was solved by small angle X-ray scattering in solution, and the structure of the first A1AO ATP synthases (from methanoarchaea) was obtained recently by single particle analyses. These studies revealed novel structural features such as a second peripheral stalk and a collar-like structure. Interestingly, the membrane-embedded electrically-driven motor (AO) is very different in archaea with sometimes novel, exceptional subunit composition.
Lewalter
Kim
K
Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt/Main, Campus Riedberg, Max-von-Laue-Str. 9, D-60438 Frankfurt/Main, Germany.
Müller
Volker
V
D000595:Amino Acid Sequence; D001105:Archaea / Q000235:genetics / Q000378:metabolism*; D019843:Archaeal Proteins / Q000502:physiology*; D005075:Biological Evolution; D018360:Crystallography, X-Ray; D004734:Energy Metabolism / Q000502:physiology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D011485:Protein Binding; D021122:Protein Subunits / Q000502:physiology; D006180:Proton-Translocating ATPases / Q000502:physiology*; D017386:Sequence Homology, Amino Acid
D019843:Archaeal Proteins; D021122:Protein Subunits; D006180:Proton-Translocating ATPases