2rrn - Revision history

OCA at 07:06, 1 May 2024

OCA — Wed, 01 May 2024 07:06:21 GMT

←Older revision		Revision as of 07:06, 1 May 2024
Line 9:		Line 9:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/SECDF_THET8 SECDF_THET8] Conducts protons, which can be regulated by a proton gradient or by binding of an unfolded protein. Proton conduction requires the large periplasmic domain of the SecD.[HAMAP-Rule:MF_01463_B] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01463_B]		[https://www.uniprot.org/uniprot/SECDF_THET8 SECDF_THET8] Conducts protons, which can be regulated by a proton gradient or by binding of an unfolded protein. Proton conduction requires the large periplasmic domain of the SecD.[HAMAP-Rule:MF_01463_B] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01463_B]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Protein translocation across the bacterial membrane, mediated by the secretory translocon SecYEG and the SecA ATPase, is enhanced by proton motive force and membrane-integrated SecDF, which associates with SecYEG. The role of SecDF has remained unclear, although it is proposed to function in later stages of translocation as well as in membrane protein biogenesis. Here, we determined the crystal structure of Thermus thermophilus SecDF at 3.3 A resolution, revealing a pseudo-symmetrical, 12-helix transmembrane domain belonging to the RND superfamily and two major periplasmic domains, P1 and P4. Higher-resolution analysis of the periplasmic domains suggested that P1, which binds an unfolded protein, undergoes functionally important conformational changes. In vitro analyses identified an ATP-independent step of protein translocation that requires both SecDF and proton motive force. Electrophysiological analyses revealed that SecDF conducts protons in a manner dependent on pH and the presence of an unfolded protein, with conserved Asp and Arg residues at the transmembrane interface between SecD and SecF playing essential roles in the movements of protons and preproteins. Therefore, we propose that SecDF functions as a membrane-integrated chaperone, powered by proton motive force, to achieve ATP-independent protein translocation.
-
-	Structure and function of a membrane component SecDF that enhances protein export.,Tsukazaki T, Mori H, Echizen Y, Ishitani R, Fukai S, Tanaka T, Perederina A, Vassylyev DG, Kohno T, Maturana AD, Ito K, Nureki O Nature. 2011 May 11;474(7350):235-8. doi: 10.1038/nature09980. PMID:21562494<ref>PMID:21562494</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2rrn" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 01:18, 28 December 2023

OCA — Thu, 28 Dec 2023 01:18:24 GMT

←Older revision		Revision as of 01:18, 28 December 2023
Line 1:		Line 1:

	==Solution structure of SecDF periplasmic domain P4==		==Solution structure of SecDF periplasmic domain P4==
-	<StructureSection load='2rrn' size='340' side='right'caption='[[2rrn~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2rrn' size='340' side='right'caption='[[2rrn]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2rrn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Thet8 Thet8~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RRN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2rrn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RRN FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'>[[3aqo\|3aqo]], [[3aqp\|3aqp]]</div~~></td></tr>	+	</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=2rrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrn OCA], [https://pdbe.org/2rrn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rrn RCSB], [https://www.ebi.ac.uk/pdbsum/2rrn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrn 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=2rrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrn OCA], [https://pdbe.org/2rrn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rrn RCSB], [https://www.ebi.ac.uk/pdbsum/2rrn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SECDF_THET8 SECDF_THET8]] Conducts protons, which can be regulated by a proton gradient or by binding of an unfolded protein. Proton conduction requires the large periplasmic domain of the SecD.[HAMAP-Rule:MF_01463_B] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01463_B]	+	[https://www.uniprot.org/uniprot/SECDF_THET8 SECDF_THET8] Conducts protons, which can be regulated by a proton gradient or by binding of an unfolded protein. Proton conduction requires the large periplasmic domain of the SecD.[HAMAP-Rule:MF_01463_B] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01463_B]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Thet8~~]]	+	[[Category: Thermus thermophilus HB8]]
-	[[Category: Echizen, Y]]	+	[[Category: Echizen Y]]
-	[[Category: Kohno, T]]	+	[[Category: Kohno T]]
-	[[Category: Nureki, O]]	+	[[Category: Nureki O]]
-	[[Category: Tanaka, T]]	+	[[Category: Tanaka T]]
-	[[Category: Tsukazaki, T]]	+	[[Category: Tsukazaki T]]
-	~~[[Category: Periplasmic domain]]~~	+
-	~~[[Category: Protein transport]]~~	+
-	~~[[Category: Secdf~~]]	+

OCA at 12:25, 23 March 2022

OCA — Wed, 23 Mar 2022 12:25:54 GMT

←Older revision		Revision as of 12:25, 23 March 2022
Line 3:		Line 3:
	<StructureSection load='2rrn' size='340' side='right'caption='[[2rrn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2rrn' size='340' side='right'caption='[[2rrn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2rrn]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Thet8 Thet8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2RRN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2rrn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RRN FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3aqo\|3aqo]], [[3aqp\|3aqp]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3aqo\|3aqo]], [[3aqp\|3aqp]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2rrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrn OCA], [~~http~~://pdbe.org/2rrn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2rrn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2rrn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrn 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=2rrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrn OCA], [https://pdbe.org/2rrn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rrn RCSB], [https://www.ebi.ac.uk/pdbsum/2rrn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SECDF_THET8 SECDF_THET8]] Conducts protons, which can be regulated by a proton gradient or by binding of an unfolded protein. Proton conduction requires the large periplasmic domain of the SecD.[HAMAP-Rule:MF_01463_B] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01463_B]	+	[[https://www.uniprot.org/uniprot/SECDF_THET8 SECDF_THET8]] Conducts protons, which can be regulated by a proton gradient or by binding of an unfolded protein. Proton conduction requires the large periplasmic domain of the SecD.[HAMAP-Rule:MF_01463_B] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01463_B]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 11:04, 17 June 2020

OCA — Wed, 17 Jun 2020 11:04:58 GMT

←Older revision		Revision as of 11:04, 17 June 2020
Line 1:		Line 1:

	==Solution structure of SecDF periplasmic domain P4==		==Solution structure of SecDF periplasmic domain P4==
-	<StructureSection load='2rrn' size='340' side='right' caption='[[2rrn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2rrn' size='340' side='right'caption='[[2rrn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2rrn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2RRN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2rrn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2RRN FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3aqo\|3aqo]], [[3aqp\|3aqp]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3aqo\|3aqo]], [[3aqp\|3aqp]]</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=2rrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrn OCA], [http://pdbe.org/2rrn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rrn RCSB], [http://www.ebi.ac.uk/pdbsum/2rrn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrn ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2rrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrn OCA], [http://pdbe.org/2rrn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rrn RCSB], [http://www.ebi.ac.uk/pdbsum/2rrn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 22:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Thet8]]		[[Category: Thet8]]
	[[Category: Echizen, Y]]		[[Category: Echizen, Y]]

OCA at 10:50, 5 August 2016

OCA — Fri, 05 Aug 2016 10:50:29 GMT

←Older revision		Revision as of 10:50, 5 August 2016
Line 1:		Line 1:
		+
	==Solution structure of SecDF periplasmic domain P4==		==Solution structure of SecDF periplasmic domain P4==
	<StructureSection load='2rrn' size='340' side='right' caption='[[2rrn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2rrn' size='340' side='right' caption='[[2rrn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2rrn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermus_thermophilus Thermus thermophilus~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RRN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2rrn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RRN FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3aqo\|3aqo]], [[3aqp\|3aqp]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3aqo\|3aqo]], [[3aqp\|3aqp]]</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=2rrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rrn RCSB], [http://www.ebi.ac.uk/pdbsum/2rrn 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=2rrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrn OCA], [http://pdbe.org/2rrn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rrn RCSB], [http://www.ebi.ac.uk/pdbsum/2rrn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrn ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SECDF_THET8 SECDF_THET8]] Conducts protons, which can be regulated by a proton gradient or by binding of an unfolded protein. Proton conduction requires the large periplasmic domain of the SecD.[HAMAP-Rule:MF_01463_B] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01463_B]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		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 2rrn" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Thermus thermophilus~~]]	+	[[Category: Thet8]]
	[[Category: Echizen, Y]]		[[Category: Echizen, Y]]
	[[Category: Kohno, T]]		[[Category: Kohno, T]]

OCA at 21:25, 3 January 2015

OCA — Sat, 03 Jan 2015 21:25:17 GMT

←Older revision		Revision as of 21:25, 3 January 2015
Line 2:		Line 2:
	<StructureSection load='2rrn' size='340' side='right' caption='[[2rrn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2rrn' size='340' side='right' caption='[[2rrn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2rrn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA]. <br>	+	<table><tr><td colspan='2'>[[2rrn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RRN FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3aqo\|3aqo]], [[3aqp\|3aqp]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3aqo\|3aqo]], [[3aqp\|3aqp]]</td></tr>
-	<tr~~><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class~~='~~plainlinks~~'~~>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2rrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rrn RCSB], [http://www.ebi.ac.uk/pdbsum/2rrn PDBsum]</span></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=2rrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rrn RCSB], [http://www.ebi.ac.uk/pdbsum/2rrn 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 13:		Line 12:
	Structure and function of a membrane component SecDF that enhances protein export.,Tsukazaki T, Mori H, Echizen Y, Ishitani R, Fukai S, Tanaka T, Perederina A, Vassylyev DG, Kohno T, Maturana AD, Ito K, Nureki O Nature. 2011 May 11;474(7350):235-8. doi: 10.1038/nature09980. PMID:21562494<ref>PMID:21562494</ref>		Structure and function of a membrane component SecDF that enhances protein export.,Tsukazaki T, Mori H, Echizen Y, Ishitani R, Fukai S, Tanaka T, Perederina A, Vassylyev DG, Kohno T, Maturana AD, Ito K, Nureki O Nature. 2011 May 11;474(7350):235-8. doi: 10.1038/nature09980. PMID:21562494<ref>PMID:21562494</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 ==
Line 20:		Line 19:
	</StructureSection>		</StructureSection>
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus]]
-	[[Category: Echizen, Y.]]	+	[[Category: Echizen, Y]]
-	[[Category: Kohno, T.]]	+	[[Category: Kohno, T]]
-	[[Category: Nureki, O.]]	+	[[Category: Nureki, O]]
-	[[Category: Tanaka, T.]]	+	[[Category: Tanaka, T]]
-	[[Category: Tsukazaki, T.]]	+	[[Category: Tsukazaki, T]]
	[[Category: Periplasmic domain]]		[[Category: Periplasmic domain]]
	[[Category: Protein transport]]		[[Category: Protein transport]]
	[[Category: Secdf]]		[[Category: Secdf]]

OCA at 08:37, 7 May 2014

OCA — Wed, 07 May 2014 08:37:54 GMT

←Older revision		Revision as of 08:37, 7 May 2014
Line 1:		Line 1:
-	[[~~Image:~~2rrn.~~png~~\|~~left~~\|~~200px~~]]	+	==Solution structure of SecDF periplasmic domain P4==
		+	<StructureSection load='2rrn' size='340' side='right' caption='[[2rrn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2rrn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3aqo\|3aqo]], [[3aqp\|3aqp]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></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=2rrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rrn RCSB], [http://www.ebi.ac.uk/pdbsum/2rrn PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Protein translocation across the bacterial membrane, mediated by the secretory translocon SecYEG and the SecA ATPase, is enhanced by proton motive force and membrane-integrated SecDF, which associates with SecYEG. The role of SecDF has remained unclear, although it is proposed to function in later stages of translocation as well as in membrane protein biogenesis. Here, we determined the crystal structure of Thermus thermophilus SecDF at 3.3 A resolution, revealing a pseudo-symmetrical, 12-helix transmembrane domain belonging to the RND superfamily and two major periplasmic domains, P1 and P4. Higher-resolution analysis of the periplasmic domains suggested that P1, which binds an unfolded protein, undergoes functionally important conformational changes. In vitro analyses identified an ATP-independent step of protein translocation that requires both SecDF and proton motive force. Electrophysiological analyses revealed that SecDF conducts protons in a manner dependent on pH and the presence of an unfolded protein, with conserved Asp and Arg residues at the transmembrane interface between SecD and SecF playing essential roles in the movements of protons and preproteins. Therefore, we propose that SecDF functions as a membrane-integrated chaperone, powered by proton motive force, to achieve ATP-independent protein translocation.

-	~~<!--~~	+	Structure and function of a membrane component SecDF that enhances protein export.,Tsukazaki T, Mori H, Echizen Y, Ishitani R, Fukai S, Tanaka T, Perederina A, Vassylyev DG, Kohno T, Maturana AD, Ito K, Nureki O Nature. 2011 May 11;474(7350):235-8. doi: 10.1038/nature09980. PMID:21562494<ref>PMID:21562494</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_2rrn"~~, ~~creates the "Structure Box" on the page~~.	+
-	~~You may change the PDB parameter~~ (~~which sets the PDB file loaded into the applet~~)	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display.~~	+
-	-->	+
-	~~{{STRUCTURE_2rrn\| PDB=2rrn \| SCENE= }}~~	+

-	~~===Solution structure~~ of ~~SecDF periplasmic domain P4===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_21562494}}, adds~~ the ~~Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 21562494 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_21562494}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2rrn]] is a 1 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:021562494<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus]]
	[[Category: Echizen, Y.]]		[[Category: Echizen, Y.]]

OCA at 06:01, 28 December 2011

OCA — Wed, 28 Dec 2011 06:01:11 GMT

←Older revision		Revision as of 06:01, 28 December 2011
Line 1:		Line 1:
-	[[Image:2rrn.~~jpg~~\|left\|200px]]	+	[[Image:2rrn.png\|left\|200px]]

	<!--		<!--
Line 11:		Line 11:
	===Solution structure of SecDF periplasmic domain P4===		===Solution structure of SecDF periplasmic domain P4===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21562494}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21562494 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21562494}}

	==About this Structure==		==About this Structure==
	[[2rrn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA].		[[2rrn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021562494</ref><references group="xtra"/>
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus]]
	[[Category: Echizen, Y.]]		[[Category: Echizen, Y.]]
Line 20:		Line 29:
	[[Category: Tanaka, T.]]		[[Category: Tanaka, T.]]
	[[Category: Tsukazaki, T.]]		[[Category: Tsukazaki, T.]]
		+	[[Category: Periplasmic domain]]
		+	[[Category: Protein transport]]
		+	[[Category: Secdf]]

OCA at 05:48, 18 May 2011

OCA — Wed, 18 May 2011 05:48:01 GMT

←Older revision		Revision as of 05:48, 18 May 2011
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-	~~'''Unreleased structure'''~~	+	[[Image:2rrn.jpg\|left\|200px]]

-	The ~~entry 2rrn~~ is ~~ON HOLD~~ ~~until Jan 29 2013~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_2rrn", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_2rrn\| PDB=2rrn \| SCENE= }}

-	~~Authors: Tanaka, T., Tsukazaki, T., Echizen, Y., Nureki, O., Kohno, T.~~	+	===Solution structure of SecDF periplasmic domain P4===

-	~~Description: Solution~~ structure ~~of SecDF periplasmic domain P4~~	+
		+	==About this Structure==
		+	[[2rrn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRN OCA].
		+	[[Category: Thermus thermophilus]]
		+	[[Category: Echizen, Y.]]
		+	[[Category: Kohno, T.]]
		+	[[Category: Nureki, O.]]
		+	[[Category: Tanaka, T.]]
		+	[[Category: Tsukazaki, T.]]

OCA at 09:27, 23 February 2011

OCA — Wed, 23 Feb 2011 09:27:56 GMT

←Older revision		Revision as of 09:27, 23 February 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 2rrn is ON HOLD	+	The entry 2rrn is ON HOLD until Jan 29 2013

	Authors: Tanaka, T., Tsukazaki, T., Echizen, Y., Nureki, O., Kohno, T.		Authors: Tanaka, T., Tsukazaki, T., Echizen, Y., Nureki, O., Kohno, T.

	Description: Solution structure of SecDF periplasmic domain P4		Description: Solution structure of SecDF periplasmic domain P4