9ity

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "9ity" [edit=sysop:move=sysop])
Current revision (06:35, 19 March 2025) (edit) (undo)
 
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 9ity is ON HOLD until Paper Publication
+
==Chloroflexus aurantiacus ADP-bound ATP synthase, state 2, focused refinement of FO and peripheral stalk==
-
 
+
<StructureSection load='9ity' size='340' side='right'caption='[[9ity]], [[Resolution|resolution]] 4.95&Aring;' scene=''>
-
Authors:
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[9ity]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Chloroflexus_aurantiacus_J-10-fl Chloroflexus aurantiacus J-10-fl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9ITY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9ITY FirstGlance]. <br>
-
Description:
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.95&#8491;</td></tr>
-
[[Category: Unreleased Structures]]
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9ity FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ity OCA], [https://pdbe.org/9ity PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ity RCSB], [https://www.ebi.ac.uk/pdbsum/9ity PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ity ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ATPF_CHLAA ATPF_CHLAA] 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.[HAMAP-Rule:MF_01398] Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).[HAMAP-Rule:MF_01398]
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Chloroflexus aurantiacus J-10-fl]]
 +
[[Category: Large Structures]]
 +
[[Category: Wu J]]
 +
[[Category: Xu X]]
 +
[[Category: Zhang X]]

Current revision

Chloroflexus aurantiacus ADP-bound ATP synthase, state 2, focused refinement of FO and peripheral stalk

PDB ID 9ity

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools