5t4o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5t4o is ON HOLD until Paper Publication
+
==Autoinhibited E. coli ATP synthase state 1==
-
 
+
<StructureSection load='5t4o' size='340' side='right' caption='[[5t4o]], [[Resolution|resolution]] 6.90&Aring;' scene=''>
-
Authors:
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[5t4o]] is a 22 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T4O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T4O FirstGlance]. <br>
-
Description:
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
-
[[Category: Unreleased Structures]]
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5t4p|5t4p]], [[5t4q|5t4q]]</td></tr>
 +
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5t4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t4o OCA], [http://pdbe.org/5t4o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t4o RCSB], [http://www.ebi.ac.uk/pdbsum/5t4o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t4o ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/ATP6_ECO55 ATP6_ECO55]] Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. [[http://www.uniprot.org/uniprot/ATPG_ECO45 ATPG_ECO45]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. [[http://www.uniprot.org/uniprot/ATPD_ECO45 ATPD_ECO45]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. [[http://www.uniprot.org/uniprot/ATPB_ECO45 ATPB_ECO45]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. [[http://www.uniprot.org/uniprot/ATPL_ECO7I ATPL_ECO7I]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. [[http://www.uniprot.org/uniprot/ATPA_ECO45 ATPA_ECO45]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. [[http://www.uniprot.org/uniprot/ATPE_ECO45 ATPE_ECO45]] Produces ATP from ADP in the presence of a proton gradient across the membrane. [[http://www.uniprot.org/uniprot/ATPF_ECO57 ATPF_ECO57]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Ishmukhametov, R]]
 +
[[Category: Sandin, S]]
 +
[[Category: Smits, C]]
 +
[[Category: Sobti, M]]
 +
[[Category: Stewart, A G]]
 +
[[Category: Stock, D]]
 +
[[Category: Wong, A S.W]]
 +
[[Category: Atp synthase]]
 +
[[Category: Atpase]]
 +
[[Category: Hydrolase]]
 +
[[Category: Membrane protein]]
 +
[[Category: Rotary motor]]

Revision as of 16:29, 2 January 2017

Autoinhibited E. coli ATP synthase state 1

5t4o, resolution 6.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools