2d00

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2d00" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d00, resolution 2.2&Aring;" /> '''Subunit F of V-type A...)
Line 1: Line 1:
-
[[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==
Line 14: Line 14:
[[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.]]
Line 32: Line 32:
[[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''

Revision as of 14:54, 21 February 2008


2d00, resolution 2.2Å

Drag the structure with the mouse to rotate

Subunit F of V-type ATPase/synthase

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.

About this Structure

2D00 is a Single protein structure of sequence from Thermus thermophilus with as ligand. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.

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:16281059

Page seeded by OCA on Thu Feb 21 16:54:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools