Sandbox Reserved 494: Difference between revisions
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Strucutre of ATP synthases are basically similiar whatever the source. In their simplest form in prokaryotes, they contain eight different subunits, with stoichiometry α<sub>3</sub>β<sub>3</sub>γδεab<sub>2</sub>c<sub>10-15</sub>. The total molecular size is about 530kDa<ref name="MM">PMID: 11997128</ref>. The enzyme consists of the extramembranous F<sub>1</sub> catalytic domain linked by means of a central stalk to an intrinsic membrane domain called F<sub>0</sub>. In the atomic structure of F<sub>1</sub>, the α and β subunits are arranged alternately around a coiled coil of two antiparallel α helices in the γ subunit <ref name="CV"> PMID: 19489730</ref>.The catalytic sites are in the β subunits at the α/β subunit interface. The remainder of the γ subunit protrudes from the α<sub>3</sub>β<sub>3</sub> assembly and can be cross linked to the polar loop region of the c subunits in F<sub>0</sub>. In mitochondria, the δ and ε subunits are associated with the γ subunit in the central stalk assembly, as are the bacterial and chloroplast ε subunits, the counterparts of mitochondrial δ. ATP-dependent rotation of γ and ε within an immobilized α<sub>3</sub>β<sub>3</sub> complex from the thermophilic bacterium '''<FONT COLOR="#F535AA">''Bacillus'' PS3</FONT>''' has been observed directly. | Strucutre of ATP synthases are basically similiar whatever the source. In their simplest form in prokaryotes, they contain eight different subunits, with stoichiometry α<sub>3</sub>β<sub>3</sub>γδεab<sub>2</sub>c<sub>10-15</sub>. The total molecular size is about 530kDa<ref name="MM">PMID: 11997128</ref>. The enzyme consists of the extramembranous F<sub>1</sub> catalytic domain linked by means of a central stalk to an intrinsic membrane domain called F<sub>0</sub>. In the atomic structure of F<sub>1</sub>, the α and β subunits are arranged alternately around a coiled coil of two antiparallel α helices in the γ subunit <ref name="CV"> PMID: 19489730</ref>.The catalytic sites are in the β subunits at the α/β subunit interface. The remainder of the γ subunit protrudes from the α<sub>3</sub>β<sub>3</sub> assembly and can be cross linked to the polar loop region of the c subunits in F<sub>0</sub>. In mitochondria, the δ and ε subunits are associated with the γ subunit in the central stalk assembly, as are the bacterial and chloroplast ε subunits, the counterparts of mitochondrial δ. ATP-dependent rotation of γ and ε within an immobilized α<sub>3</sub>β<sub>3</sub> complex from the thermophilic bacterium '''<FONT COLOR="#F535AA">''Bacillus'' PS3</FONT>''' has been observed directly. | ||
[[Image:1c17_dimor_(3).jpg | thumb|frame|Two structural domains of ATP synthase | [[Image:1c17_dimor_(3).jpg | thumb|frame|Two structural domains of ATP synthase<ref name="CV" />.]] | ||
==High resolution structure analysis== | ==High resolution structure analysis== | ||
