2d00: Difference between revisions

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New page: left|200px<br /><applet load="2d00" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d00, resolution 2.2Å" /> '''Subunit F of V-type A...
 
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[[Image:2d00.gif|left|200px]]<br /><applet load="2d00" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2d00.gif|left|200px]]<br /><applet load="2d00" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2d00, resolution 2.2&Aring;" />
caption="2d00, resolution 2.2&Aring;" />
'''Subunit F of V-type ATPase/synthase'''<br />
'''Subunit F of V-type ATPase/synthase'''<br />


==Overview==
==Overview==
The crystal structure of subunit F of vacuole-type ATPase/synthase, (prokaryotic V-ATPase) was determined to of 2.2 A resolution. The subunit, reveals unexpected structural similarity to the response regulator, proteins that include the Escherichia coli chemotaxis response regulator, CheY. The structure was successfully placed into the low-resolution EM, structure of the prokaryotic holo-V-ATPase at a location indicated by the, results of crosslinking experiments. The crystal structure, together with, the single-molecule analysis using fluorescence resonance energy transfer, showed that the subunit F exhibits two conformations, a 'retracted' form, in the absence and an 'extended' form in the presence of ATP. Our results, postulated that the subunit F is a regulatory subunit in the V-ATPase.
The crystal structure of subunit F of vacuole-type ATPase/synthase (prokaryotic V-ATPase) was determined to of 2.2 A resolution. The subunit reveals unexpected structural similarity to the response regulator proteins that include the Escherichia coli chemotaxis response regulator CheY. The structure was successfully placed into the low-resolution EM structure of the prokaryotic holo-V-ATPase at a location indicated by the results of crosslinking experiments. The crystal structure, together with the single-molecule analysis using fluorescence resonance energy transfer, showed that the subunit F exhibits two conformations, a 'retracted' form in the absence and an 'extended' form in the presence of ATP. Our results postulated that the subunit F is a regulatory subunit in the V-ATPase.


==About this Structure==
==About this Structure==
2D00 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D00 OCA].  
2D00 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D00 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Bernal, R.A.]]
[[Category: Bernal, R A.]]
[[Category: Carpenter, E.P.]]
[[Category: Carpenter, E P.]]
[[Category: Iino, R.]]
[[Category: Iino, R.]]
[[Category: Ikeda, C.]]
[[Category: Ikeda, C.]]
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[[Category: v-atpase]]
[[Category: v-atpase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:22:22 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:01 2008''