4cbj - Revision history

OCA at 12:07, 20 December 2023

OCA — Wed, 20 Dec 2023 12:07:07 GMT

←Older revision		Revision as of 12:07, 20 December 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cbj]] 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=4CBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CBJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cbj]] 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=4CBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CBJ 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=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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]] 2.8Å</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=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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=4cbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbj OCA], [https://pdbe.org/4cbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbj RCSB], [https://www.ebi.ac.uk/pdbsum/4cbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbj ProSAT]</span></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=4cbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbj OCA], [https://pdbe.org/4cbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbj RCSB], [https://www.ebi.ac.uk/pdbsum/4cbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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]	+	[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]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	In the c-ring rotor of ATP synthases ions are shuttled across the membrane during ATP synthesis by a unique rotary mechanism. We investigated characteristics of the c-ring from the alkaliphile Bacillus pseudofirmus OF4 with respect to evolutionary adaptations to operate with protons at high environmental pH. The X-ray structures of the wild-type c13 ring at pH 9.0 and a 'neutralophile-like' mutant (P51A) at pH 4.4, at 2.4 and 2.8 A resolution, respectively, reveal a dependency of the conformation and protonation state of the proton-binding glutamate (E54 ) on environmental hydrophobicity. Faster labeling kinetics with the inhibitor dicyclohexylcarbodiimide (DCCD) demonstrate a greater flexibility of E54 in the mutant due to reduced water occupancy within the H+ -binding site. A second 'neutralophile-like' mutant (V21N) shows reduced growth at high pH, which is explained by restricted conformational freedom of the mutant's E54 carboxylate. The study directly connects subtle structural adaptations of the c-ring ion-binding site to in vivo effects of alkaliphile cell physiology.
		+
		+	The c-ring ion-binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle.,Preiss L, Langer JD, Hicks DB, Liu J, Yildiz O, Krulwich TA, Meier T Mol Microbiol. 2014 Apr 8. doi: 10.1111/mmi.12605. PMID:24707994<ref>PMID:24707994</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4cbj" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[ATPase 3D structures\|ATPase 3D structures]]		*[[ATPase 3D structures\|ATPase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:36, 7 September 2022

OCA — Wed, 07 Sep 2022 17:36:51 GMT

←Older revision		Revision as of 17:36, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4cbj' size='340' side='right'caption='[[4cbj]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='4cbj' size='340' side='right'caption='[[4cbj]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4cbj]] is a 13 chain structure with sequence from [~~http~~://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=4CBJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4CBJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4cbj]] 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=4CBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CBJ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPV:DODECYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>DPV</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene>~~</td></tr>~~	+	</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=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbj OCA], [https://pdbe.org/4cbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbj RCSB], [https://www.ebi.ac.uk/pdbsum/4cbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbj ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cbk\|4cbk]]~~</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=4cbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbj OCA], [~~http~~://pdbe.org/4cbj PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4cbj RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4cbj PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbj ProSAT]</span></td></tr>	+
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[[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]
-	~~In the c-ring rotor of~~ ATP ~~synthases ions are shuttled across the membrane during~~ ATP ~~synthesis by a unique rotary mechanism. We investigated characteristics of the c-ring~~ from the ~~alkaliphile Bacillus pseudofirmus OF4 with respect to evolutionary adaptations to operate with protons at high environmental pH~~. ~~The X~~-~~ray structures~~ of the ~~wild-type c13 ring at pH 9.0~~ and ~~a 'neutralophile-like' mutant~~ (~~P51A~~) ~~at pH 4.4~~, ~~at 2.4~~ and 2.~~8 A resolution~~, ~~respectively, reveal a dependency of~~ the ~~conformation and protonation state~~ of ~~the proton-binding glutamate~~ (~~E54~~ ) ~~on environmental hydrophobicity. Faster labeling kinetics with the inhibitor dicyclohexylcarbodiimide (DCCD) demonstrate~~ a ~~greater flexibility~~ of ~~E54 in~~ the ~~mutant due~~ to ~~reduced water occupancy within the H+ -binding site~~. ~~A second 'neutralophile~~-~~like' mutant~~ (~~V21N~~) ~~shows reduced growth at high pH, which is explained by restricted conformational freedom of~~ the ~~mutant's E54 carboxylate~~. ~~The study directly connects subtle structural adaptations of the~~ c-ring ~~ion-binding site to in vivo effects~~ of ~~alkaliphile cell physiology.~~	+
-		+
-	~~The c~~-~~ring ion-binding site of~~ the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle.,Preiss L, Langer JD, Hicks DB, Liu J, Yildiz O, Krulwich TA, Meier T Mol Microbiol. 2014 Apr 8. doi: 10.1111/mmi.12605. PMID:24707994<ref>PMID:24707994</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of~~ the U.~~S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe~~-~~citations 4cbj" style="background-color~~:~~#fffaf0;"></div>~~	+

	==See Also==		==See Also==
-	*[[ATPase\|ATPase]]	+	*[[ATPase 3D structures\|ATPase 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ pseudofirmus ~~of4~~]]	+	[[Category: Alkalihalophilus pseudofirmus OF4]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Meier, T]]	+	[[Category: Meier T]]
-	[[Category: Preiss, L]]	+	[[Category: Preiss L]]
-	[[Category: Yildiz, O]]	+	[[Category: Yildiz O]]
-	~~[[Category: C-ring rotor]]~~	+
-	~~[[Category: F1fo-atp synthase]]~~	+
-	~~[[Category: Ion binding pocket]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 08:58, 20 March 2019

OCA — Wed, 20 Mar 2019 08:58:29 GMT

←Older revision		Revision as of 08:58, 20 March 2019
Line 1:		Line 1:

	==The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology==		==The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology==
-	<StructureSection load='4cbj' size='340' side='right' caption='[[4cbj]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='4cbj' size='340' side='right'caption='[[4cbj]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cbj]] is a 13 chain structure with sequence from [http://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=4CBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cbj]] is a 13 chain structure with sequence from [http://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=4CBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBJ FirstGlance]. <br>
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Bacillus pseudofirmus of4]]		[[Category: Bacillus pseudofirmus of4]]
		+	[[Category: Large Structures]]
	[[Category: Meier, T]]		[[Category: Meier, T]]
	[[Category: Preiss, L]]		[[Category: Preiss, L]]

OCA at 16:01, 11 August 2016

OCA — Thu, 11 Aug 2016 16:01:32 GMT

←Older revision		Revision as of 16:01, 11 August 2016
Line 1:		Line 1:
		+
	==The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology==		==The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology==
	<StructureSection load='4cbj' size='340' side='right' caption='[[4cbj]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='4cbj' size='340' side='right' caption='[[4cbj]], [[Resolution\|resolution]] 2.80Å' scene=''>
Line 6:		Line 7:
	<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='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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cbk\|4cbk]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cbk\|4cbk]]</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=4cbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbj RCSB], [http://www.ebi.ac.uk/pdbsum/4cbj PDBsum]</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=4cbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbj OCA], [http://pdbe.org/4cbj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cbj RCSB], [http://www.ebi.ac.uk/pdbsum/4cbj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbj ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 16:		Line 17:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4cbj" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[ATPase\|ATPase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:29, 4 January 2015

OCA — Sun, 04 Jan 2015 12:29:20 GMT

←Older revision		Revision as of 12:29, 4 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cbj]] is a 13 chain structure with sequence from [http://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=4CBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cbj]] is a 13 chain structure with sequence from [http://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=4CBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBJ FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPV:DODECYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>DPV</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPV:DODECYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>DPV</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr>
-	<tr><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='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><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cbk\|4cbk]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cbk\|4cbk]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbj RCSB], [http://www.ebi.ac.uk/pdbsum/4cbj PDBsum]</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=4cbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbj RCSB], [http://www.ebi.ac.uk/pdbsum/4cbj PDBsum]</span></td></tr>
-	<table>	+	</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 21:
	</StructureSection>		</StructureSection>
	[[Category: Bacillus pseudofirmus of4]]		[[Category: Bacillus pseudofirmus of4]]
-	[[Category: Meier, T.]]	+	[[Category: Meier, T]]
-	[[Category: Preiss, L.]]	+	[[Category: Preiss, L]]
-	[[Category: Yildiz, O.]]	+	[[Category: Yildiz, O]]
	[[Category: C-ring rotor]]		[[Category: C-ring rotor]]
	[[Category: F1fo-atp synthase]]		[[Category: F1fo-atp synthase]]
	[[Category: Ion binding pocket]]		[[Category: Ion binding pocket]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 06:45, 11 June 2014

OCA — Wed, 11 Jun 2014 06:45:47 GMT

←Older revision		Revision as of 06:45, 11 June 2014
Line 14:		Line 14:
	The c-ring ion-binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle.,Preiss L, Langer JD, Hicks DB, Liu J, Yildiz O, Krulwich TA, Meier T Mol Microbiol. 2014 Apr 8. doi: 10.1111/mmi.12605. PMID:24707994<ref>PMID:24707994</ref>		The c-ring ion-binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle.,Preiss L, Langer JD, Hicks DB, Liu J, Yildiz O, Krulwich TA, Meier T Mol Microbiol. 2014 Apr 8. doi: 10.1111/mmi.12605. PMID:24707994<ref>PMID:24707994</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
	== References ==		== References ==

OCA at 09:47, 28 May 2014

OCA — Wed, 28 May 2014 09:47:34 GMT

←Older revision		Revision as of 09:47, 28 May 2014
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-	'''~~Unreleased~~ structure'''	+	==The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology==
		+	<StructureSection load='4cbj' size='340' side='right' caption='[[4cbj]], [[Resolution\|resolution]] 2.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4cbj]] is a 13 chain structure with sequence from [http://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=4CBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBJ FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPV:DODECYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>DPV</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene><br>
		+	<tr><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><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cbk\|4cbk]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbj RCSB], [http://www.ebi.ac.uk/pdbsum/4cbj PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	In the c-ring rotor of ATP synthases ions are shuttled across the membrane during ATP synthesis by a unique rotary mechanism. We investigated characteristics of the c-ring from the alkaliphile Bacillus pseudofirmus OF4 with respect to evolutionary adaptations to operate with protons at high environmental pH. The X-ray structures of the wild-type c13 ring at pH 9.0 and a 'neutralophile-like' mutant (P51A) at pH 4.4, at 2.4 and 2.8 A resolution, respectively, reveal a dependency of the conformation and protonation state of the proton-binding glutamate (E54 ) on environmental hydrophobicity. Faster labeling kinetics with the inhibitor dicyclohexylcarbodiimide (DCCD) demonstrate a greater flexibility of E54 in the mutant due to reduced water occupancy within the H+ -binding site. A second 'neutralophile-like' mutant (V21N) shows reduced growth at high pH, which is explained by restricted conformational freedom of the mutant's E54 carboxylate. The study directly connects subtle structural adaptations of the c-ring ion-binding site to in vivo effects of alkaliphile cell physiology.

-	The ~~entry 4cbj is ON HOLD until sometime in~~ the ~~future~~	+	The c-ring ion-binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle.,Preiss L, Langer JD, Hicks DB, Liu J, Yildiz O, Krulwich TA, Meier T Mol Microbiol. 2014 Apr 8. doi: 10.1111/mmi.12605. PMID:24707994<ref>PMID:24707994</ref>

-	~~Authors~~: Preiss, L., Yildiz, O.~~, Meier, T.~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~The c~~-ring ~~ion binding site of the ATP~~ synthase ~~from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Bacillus pseudofirmus of4]]
		+	[[Category: Meier, T.]]
		+	[[Category: Preiss, L.]]
		+	[[Category: Yildiz, O.]]
		+	[[Category: C-ring rotor]]
		+	[[Category: F1fo-atp synthase]]
		+	[[Category: Ion binding pocket]]
		+	[[Category: Transferase]]

OCA at 07:24, 21 May 2014

OCA — Wed, 21 May 2014 07:24:27 GMT

←Older revision		Revision as of 07:24, 21 May 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4cbj is ON HOLD	+	The entry 4cbj is ON HOLD until sometime in the future

	Authors: Preiss, L., Yildiz, O., Meier, T.		Authors: Preiss, L., Yildiz, O., Meier, T.

	Description: The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology		Description: The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology

OCA at 07:03, 23 April 2014

OCA — Wed, 23 Apr 2014 07:03:06 GMT

←Older revision		Revision as of 07:03, 23 April 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4cbj is ON HOLD ~~until Paper Publication~~	+	The entry 4cbj is ON HOLD

	Authors: Preiss, L., Yildiz, O., Meier, T.		Authors: Preiss, L., Yildiz, O., Meier, T.

	Description: The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology		Description: The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology

OCA at 06:40, 6 November 2013

OCA — Wed, 06 Nov 2013 06:40:43 GMT

←Older revision		Revision as of 06:40, 6 November 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4cbj is ON HOLD	+	The entry 4cbj is ON HOLD until Paper Publication

	Authors: Preiss, L., Yildiz, O., Meier, T.		Authors: Preiss, L., Yildiz, O., Meier, T.

	Description: The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology		Description: The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology