1c99

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1c99" [edit=sysop:move=sysop])
Current revision (23:25, 27 December 2023) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1c99.png|left|200px]]
 
-
{{STRUCTURE_1c99| PDB=1c99 | SCENE= }}
+
==ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI==
 +
<StructureSection load='1c99' size='340' side='right'caption='[[1c99]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1c99]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C99 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c99 OCA], [https://pdbe.org/1c99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c99 RCSB], [https://www.ebi.ac.uk/pdbsum/1c99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c99 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ATPL_ECOLI ATPL_ECOLI] 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_01396] Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/1c99_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1c99 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
F1F0 ATP synthases use a transmembrane proton gradient to drive the synthesis of cellular ATP. The structure of the cytosolic F1 portion of the enzyme and the basic mechanism of ATP hydrolysis by F1 are now well established, but how proton translocation through the transmembrane F0 portion drives these catalytic changes is less clear. Here we describe the structural changes in the proton-translocating F0 subunit c that are induced by deprotonating the specific aspartic acid involved in proton transport. Conformational changes between the protonated and deprotonated forms of subunit c provide the structural basis for an explicit mechanism to explain coupling of proton translocation by F0 to the rotation of subunits within the core of F1. Rotation of these subunits within F1 causes the catalytic conformational changes in the active sites of F1 that result in ATP synthesis.
-
===ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI===
+
Structural changes linked to proton translocation by subunit c of the ATP synthase.,Rastogi VK, Girvin ME Nature. 1999 Nov 18;402(6759):263-8. PMID:10580496<ref>PMID:10580496</ref>
-
{{ABSTRACT_PUBMED_10580496}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1c99" style="background-color:#fffaf0;"></div>
-
==About this Structure==
+
==See Also==
-
[[1c99]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C99 OCA].
+
*[[ATPase 3D structures|ATPase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:010580496</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Girvin, M E.]]
+
[[Category: Large Structures]]
-
[[Category: Rastogi, V K.]]
+
[[Category: Girvin ME]]
-
[[Category: Atp synthase]]
+
[[Category: Rastogi VK]]
-
[[Category: Hydrolase]]
+
-
[[Category: Proteolipid f1fo]]
+
-
[[Category: Proton translocation]]
+
-
[[Category: Proton transport]]
+

Current revision

ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI

PDB ID 1c99

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1c99"
Personal tools