Sandbox Reserved 494: Difference between revisions

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==Structure of ATP synthase==

Strucutre of ATP synthases are basically similiar whatever the source. In their simplest form in prokaryotes, they contain eight different subunits, with stoichiometry ~~α3β~~3γδεab2c10-15. The total molecular size is about 530kDa<ref name="MM">PMID: 11997128</ref>. The enzyme consists of the extramembranous F1 catalytic domain linked by means of a central stalk to an intrinsic membrane domain called F0. In the atomic structure of F1, 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 α3β3 assembly and can be cross linked to the polar loop region of the c subunits in F0. 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 α3β3 complex from the thermophilic bacterium '''''Bacillus'' PS3''' 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 αβ3γδεab2c10-15. The total molecular size is about 530kDa<ref name="MM">PMID: 11997128</ref>. The enzyme consists of the extramembranous F1 catalytic domain linked by means of a central stalk to an intrinsic membrane domain called F0. In the atomic structure of F1, 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 α3β3 assembly and can be cross linked to the polar loop region of the c subunits in F0. 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 α3β3 complex from the thermophilic bacterium '''''Bacillus'' PS3''' has been observed directly.

[[Image:1c17_dimor_(3).jpg | thumb|frame|Two structural domains of ATP synthase<ref name="CV" />.]]

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==Perspective==

An emerging possibility of step-size mismatch between the F1 and F0 motors provides an opportunity to find a noval coupling mechanism of the two motors that will explain why the mismatch is good for the enzyme. Finally, one can even dream of using this, the world's tiniest motor, as an engine part in the fabrication of nano-machines. The marvel of ATP will continue.

As a motor protein, ATP synthase offers a rare research opportunity. Structure of the F1 motor, both rotor and stator in the same assembly, are known in atomic detail for the first time, and rotation can be analyzed at sub-millisecond time resolution. An emerging possibility of step-size mismatch between the F1 and F0 motors provides an opportunity to find a noval coupling mechanism of the two motors that will explain why the mismatch is good for the enzyme. Finally, one can even dream of using this, the world's tiniest motor, as an engine part in the fabrication of nano-machines. The marvel of ATP will continue.

==Additional Resources==

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@@ Line 7: / Line 7: @@
 ==Structure of ATP synthase==
-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 αβ<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<ref name="CV" />.]]
@@ Line 21: / Line 21: @@
 ==Perspective==
-An emerging possibility of step-size mismatch between the F<sub>1</sub> and F<sub>0</sub> motors provides an opportunity to find a noval coupling mechanism of the two motors that will explain why the mismatch is good for the enzyme. Finally, one can even dream of using this, the world's tiniest motor, as an engine part in the fabrication of nano-machines. The marvel of ATP will continue.
+As a motor protein, ATP synthase offers a rare research opportunity. Structure of the F<sub>1</sub> motor, both rotor and stator in the same assembly, are known in atomic detail for the first time, and rotation can be analyzed at sub-millisecond time resolution. An emerging possibility of step-size mismatch between the F<sub>1</sub> and F<sub>0</sub> motors provides an opportunity to find a noval coupling mechanism of the two motors that will explain why the mismatch is good for the enzyme. Finally, one can even dream of using this, the world's tiniest motor, as an engine part in the fabrication of nano-machines. The marvel of ATP will continue.
 ==Additional Resources==