2x2v

From Proteopedia

(Difference between revisions)

Revision as of 10:22, 20 December 2023

Structural basis of a novel proton-coordination type in an F1Fo-ATP synthase rotor ring

Structural highlights

2x2v is a 13 chain structure with sequence from Alkalihalophilus pseudofirmus OF4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATPL_ALKPO 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 between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We solved the crystal structure of a novel type of c-ring isolated from Bacillus pseudofirmus OF4 at 2.5 A, revealing a cylinder with a tridecameric stoichiometry, a central pore, and an overall shape that is distinct from those reported thus far. Within the groove of two neighboring c-subunits, the conserved glutamate of the outer helix shares the proton with a bound water molecule which itself is coordinated by three other amino acids of outer helices. Although none of the inner helices contributes to ion binding and the glutamate has no other hydrogen bonding partner than the water oxygen, the site remains in a stable, ion-locked conformation that represents the functional state present at the c-ring/membrane interface during rotation. This structure reveals a new, third type of ion coordination in ATP synthases. It appears in the ion binding site of an alkaliphile in which it represents a finely tuned adaptation of the proton affinity during the reaction cycle.

A new type of proton coordination in an F(1)F(o)-ATP synthase rotor ring.,Preiss L, Yildiz O, Hicks DB, Krulwich TA, Meier T PLoS Biol. 2010 Aug 3;8(8):e1000443. PMID:20689804^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Preiss L, Yildiz O, Hicks DB, Krulwich TA, Meier T. A new type of proton coordination in an F(1)F(o)-ATP synthase rotor ring. PLoS Biol. 2010 Aug 3;8(8):e1000443. PMID:20689804 doi:10.1371/journal.pbio.1000443

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2x2v"

@@ Line 3: / Line 3: @@
 <StructureSection load='2x2v' size='340' side='right'caption='[[2x2v]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2x2v]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_pseudofirmus_of4 Bacillus pseudofirmus of4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X2V FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2x2v]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalophilus_pseudofirmus_OF4 Alkalihalophilus pseudofirmus OF4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X2V FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DPV:DODECYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>DPV</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DPV:DODECYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>DPV</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=2x2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x2v OCA], [https://pdbe.org/2x2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x2v RCSB], [https://www.ebi.ac.uk/pdbsum/2x2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x2v ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ATPL_ALKPO ATPL_ALKPO] 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 between 10-14 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]]
@@ Line 34: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus pseudofirmus of4]]
+[[Category: Alkalihalophilus pseudofirmus OF4]]
 [[Category: Large Structures]]
-[[Category: Hicks, D B]]
+[[Category: Hicks DB]]
-[[Category: Krulwich, T A]]
+[[Category: Krulwich TA]]
-[[Category: Meier, T]]
+[[Category: Meier T]]
-[[Category: Preiss, L]]
+[[Category: Preiss L]]
-[[Category: Yildiz, O]]
+[[Category: Yildiz O]]
-[[Category: Atp synthesis]]
-[[Category: C-ring rotor]]
-[[Category: Hydrogen ion transport]]
-[[Category: Hydronium ion]]
-[[Category: Ion binding pocket]]
-[[Category: Ion transport]]
-[[Category: Membrane]]
-[[Category: Membrane protein]]
-[[Category: Transmembrane]]
-[[Category: Transport]]

2x2v

From Proteopedia

Revision as of 10:22, 20 December 2023

Structural basis of a novel proton-coordination type in an F1Fo-ATP synthase rotor ring

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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