Structure and function of the A1A0-ATPases from methanogenic Archaea.
Recent molecular studies revealed nine to ten gene products involved in function/assembly of the methanoarchaeal ATPase and unravel a close relationship of the A1A0-ATPase and the V1V0-ATPase with respect to subunit composition and the structure of individual subunits. Most interestingly, there is an astonishing variability in the size of the proteolipids in methanoarchaeal A1A0-ATPases with six, four, or two transmembrane helices and a variable number of conserved protonizable groups per monomer. Despite the structural similarities the A1A0-ATPase differs fundamentally from the V1V0-ATPase by its ability to synthesize ATP, a feature shared with F1F0-ATPases. The discovery of duplicated and triplicated versions of the proteolipid in A1A0-ATP synthases questions older views of the structural requirements for ATP synthases versus ATP hydrolases and sheds new light on the evolution of these secondary energy converters.
Müller
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V
Lehrstuhl für Mikrobiologie der Ludwig-Maximilians-Universität München, Germany.
Ruppert
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C
Lemker
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T
D000595:Amino Acid Sequence; D019843:Archaeal Proteins; D002384:Catalysis; D019605:Euryarchaeota / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017433:Protein Structure, Secondary; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013329:Structure-Activity Relationship
D019843:Archaeal Proteins; C113203:A1A0 ATPase, Methanosarcina mazei; D006180:Proton-Translocating ATPases