2d00: Difference between revisions

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[[Image:2d00.gif|left|200px]]<br /><applet load="2d00" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2d00.gif|left|200px]]
caption="2d00, resolution 2.2&Aring;" />
 
'''Subunit F of V-type ATPase/synthase'''<br />
{{Structure
|PDB= 2d00 |SIZE=350|CAPTION= <scene name='initialview01'>2d00</scene>, resolution 2.2&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
|ACTIVITY= [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]
|GENE=
}}
 
'''Subunit F of V-type ATPase/synthase'''
 


==Overview==
==Overview==
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==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 <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].  
2D00 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D00 OCA].  


==Reference==
==Reference==
Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus., Makyio H, Iino R, Ikeda C, Imamura H, Tamakoshi M, Iwata M, Stock D, Bernal RA, Carpenter EP, Yoshida M, Yokoyama K, Iwata S, EMBO J. 2005 Nov 16;24(22):3974-83. Epub 2005 Nov 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16281059 16281059]
Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus., Makyio H, Iino R, Ikeda C, Imamura H, Tamakoshi M, Iwata M, Stock D, Bernal RA, Carpenter EP, Yoshida M, Yokoyama K, Iwata S, EMBO J. 2005 Nov 16;24(22):3974-83. Epub 2005 Nov 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16281059 16281059]
[[Category: H(+)-transporting two-sector ATPase]]
[[Category: H(+)-transporting two-sector ATPase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: v-atpase]]
[[Category: v-atpase]]


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Revision as of 17:21, 20 March 2008

File:2d00.gif


PDB ID 2d00

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, resolution 2.2Å
Ligands:
Activity: H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Coordinates: save as pdb, mmCIF, xml



Subunit F of V-type ATPase/synthase


OverviewOverview

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 StructureAbout this Structure

2D00 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus., Makyio H, Iino R, Ikeda C, Imamura H, Tamakoshi M, Iwata M, Stock D, Bernal RA, Carpenter EP, Yoshida M, Yokoyama K, Iwata S, EMBO J. 2005 Nov 16;24(22):3974-83. Epub 2005 Nov 10. PMID:16281059

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