1r48 - Revision history

OCA at 09:03, 22 May 2024

2024-05-22T09:03:03Z

←Older revision		Revision as of 09:03, 22 May 2024
Line 19:		Line 19:
	</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=1r48 ConSurf].		</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=1r48 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Bacteria respond to increasing medium osmolality by accumulating organic solutes that are compatible with cellular functions. Transporter ProP of Escherichia coli, a proton symporter and a member of the major facilitator superfamily, senses osmotic shifts and responds by importing osmolytes such as glycine betaine. ProP contains a cytoplasmic, C-terminal extension that is essential for its activity. A peptide corresponding to the C-terminal extension of ProP forms a homodimeric alpha-helical coiled-coil even though some of its heptad a positions are not occupied by hydrophobic amino acid residues. Unexpectedly, amino acid replacement R488I, occurring at a heptad a position, destabilized the coiled-coil formed by the ProP peptide and attenuated the response of the intact transporter to osmotic upshifts in vivo. Thus, ProP was proposed to dimerize via an antiparallel coiled-coil. We used nuclear magnetic resonance (NMR) spectroscopy to determine the structure of the synthetic peptide corresponding to residues 468-497 of ProP. This region did form an antiparallel coil-coil in which critical residue R488 specifies the antiparallel coiled-coil orientation by forming stabilizing salt-bridges. Charged residues (both acidic and basic) are clustered on the c/g surface of the coiled-coil whereas polar residues are distributed on the b/e surface. This causes the structure to be bent, in contrast to other known antiparallel coiled-coils (those from the hepatitis delta antigen (PDB ID code 1A92) and the bovine F(1) ATPase inhibitor protein (PDB ID code 1HF9)). The coiled-coil and its possible importance for osmosensing are discussed.
		+
		+	Solution structure of the C-terminal antiparallel coiled-coil domain from Escherichia coli osmosensor ProP.,Zoetewey DL, Tripet BP, Kutateladze TG, Overduin MJ, Wood JM, Hodges RS J Mol Biol. 2003 Dec 12;334(5):1063-76. PMID:14643666<ref>PMID:14643666</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1r48" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:09, 17 April 2024

2024-04-17T06:09:15Z

←Older revision		Revision as of 06:09, 17 April 2024
Line 1:		Line 1:

	==Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP==		==Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP==
-	<StructureSection load='1r48' size='340' side='right'caption='[[1r48~~]], [[NMR_Ensembles_of_Models \| 51 NMR models~~]]' scene=''>	+	<StructureSection load='1r48' size='340' side='right'caption='[[1r48]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R48 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1r48]] is a 2 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=1R48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R48 FirstGlance]. <br>
-	</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=1r48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r48 OCA], [https://pdbe.org/1r48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r48 RCSB], [https://www.ebi.ac.uk/pdbsum/1r48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r48 ProSAT]</span></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=1r48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r48 OCA], [https://pdbe.org/1r48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r48 RCSB], [https://www.ebi.ac.uk/pdbsum/1r48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r48 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PROP_ECOLI PROP_ECOLI]] Proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response.	+	[https://www.uniprot.org/uniprot/PROP_ECOLI PROP_ECOLI] Proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 18:		Line 19:
	</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=1r48 ConSurf].		</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=1r48 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Bacteria respond to increasing medium osmolality by accumulating organic solutes that are compatible with cellular functions. Transporter ProP of Escherichia coli, a proton symporter and a member of the major facilitator superfamily, senses osmotic shifts and responds by importing osmolytes such as glycine betaine. ProP contains a cytoplasmic, C-terminal extension that is essential for its activity. A peptide corresponding to the C-terminal extension of ProP forms a homodimeric alpha-helical coiled-coil even though some of its heptad a positions are not occupied by hydrophobic amino acid residues. Unexpectedly, amino acid replacement R488I, occurring at a heptad a position, destabilized the coiled-coil formed by the ProP peptide and attenuated the response of the intact transporter to osmotic upshifts in vivo. Thus, ProP was proposed to dimerize via an antiparallel coiled-coil. We used nuclear magnetic resonance (NMR) spectroscopy to determine the structure of the synthetic peptide corresponding to residues 468-497 of ProP. This region did form an antiparallel coil-coil in which critical residue R488 specifies the antiparallel coiled-coil orientation by forming stabilizing salt-bridges. Charged residues (both acidic and basic) are clustered on the c/g surface of the coiled-coil whereas polar residues are distributed on the b/e surface. This causes the structure to be bent, in contrast to other known antiparallel coiled-coils (those from the hepatitis delta antigen (PDB ID code 1A92) and the bovine F(1) ATPase inhibitor protein (PDB ID code 1HF9)). The coiled-coil and its possible importance for osmosensing are discussed.
-
-	Solution structure of the C-terminal antiparallel coiled-coil domain from Escherichia coli osmosensor ProP.,Zoetewey DL, Tripet BP, Kutateladze TG, Overduin MJ, Wood JM, Hodges RS J Mol Biol. 2003 Dec 12;334(5):1063-76. PMID:14643666<ref>PMID:14643666</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1r48" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hodges~~, R S~~]]	+	[[Category: Hodges RS]]
-	[[Category: Kutateladze~~, T G~~]]	+	[[Category: Kutateladze TG]]
-	[[Category: Overduin~~, M J~~]]	+	[[Category: Overduin MJ]]
-	[[Category: Tripet~~, B P~~]]	+	[[Category: Tripet BP]]
-	[[Category: Wood~~, J M~~]]	+	[[Category: Wood JM]]
-	[[Category: Zoetewey~~, D L]]~~	+	[[Category: Zoetewey DL]]
-	~~[[Category: Antiparallel]]~~	+
-	~~[[Category: Coiled-coil]]~~	+
-	~~[[Category: Cytoplasmic]]~~	+
-	~~[[Category: Osmosensor]]~~	+
-	~~[[Category: Transport protein]]~~	+
-	~~[[Category: Two-stranded homodimer~~]]	+

OCA at 10:07, 15 September 2021

2021-09-15T10:07:53Z

←Older revision		Revision as of 10:07, 15 September 2021
Line 3:		Line 3:
	<StructureSection load='1r48' size='340' side='right'caption='[[1r48]], [[NMR_Ensembles_of_Models \| 51 NMR models]]' scene=''>		<StructureSection load='1r48' size='340' side='right'caption='[[1r48]], [[NMR_Ensembles_of_Models \| 51 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1R48 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R48 FirstGlance]. <br>
-	</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=1r48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r48 OCA], [~~http~~://pdbe.org/1r48 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1r48 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1r48 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1r48 ProSAT]</span></td></tr>	+	</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=1r48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r48 OCA], [https://pdbe.org/1r48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r48 RCSB], [https://www.ebi.ac.uk/pdbsum/1r48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r48 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PROP_ECOLI PROP_ECOLI]] Proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response.	+	[[https://www.uniprot.org/uniprot/PROP_ECOLI PROP_ECOLI]] Proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 11:51, 4 December 2019

2019-12-04T11:51:02Z

←Older revision		Revision as of 11:51, 4 December 2019
Line 1:		Line 1:

	==Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP==		==Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP==
-	<StructureSection load='1r48' size='340' side='right' caption='[[1r48]], [[NMR_Ensembles_of_Models \| 51 NMR models]]' scene=''>	+	<StructureSection load='1r48' size='340' side='right'caption='[[1r48]], [[NMR_Ensembles_of_Models \| 51 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R48 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R48 FirstGlance]. <br>
Line 31:		Line 31:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Hodges, R S]]		[[Category: Hodges, R S]]
	[[Category: Kutateladze, T G]]		[[Category: Kutateladze, T G]]

OCA at 08:14, 28 February 2018

2018-02-28T08:14:56Z

←Older revision		Revision as of 08:14, 28 February 2018
Line 1:		Line 1:
		+
	==Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP==		==Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP==
	<StructureSection load='1r48' size='340' side='right' caption='[[1r48]], [[NMR_Ensembles_of_Models \| 51 NMR models]]' scene=''>		<StructureSection load='1r48' size='340' side='right' caption='[[1r48]], [[NMR_Ensembles_of_Models \| 51 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R48 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R48 FirstGlance]. <br>
-	</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=1r48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r48 OCA], [http://pdbe.org/1r48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r48 RCSB], [http://www.ebi.ac.uk/pdbsum/1r48 PDBsum]</span></td></tr>	+	</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=1r48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r48 OCA], [http://pdbe.org/1r48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r48 RCSB], [http://www.ebi.ac.uk/pdbsum/1r48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r48 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 11:		Line 12:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r4/1r48_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r4/1r48_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 14:01, 7 February 2016

2016-02-07T14:01:07Z

←Older revision		Revision as of 14:01, 7 February 2016
Line 15:		Line 15:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=1r48 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 02:10, 10 September 2015

2015-09-10T02:10:45Z

←Older revision		Revision as of 02:10, 10 September 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R48 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R48 FirstGlance]. <br>
-	</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=1r48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1r48 RCSB], [http://www.ebi.ac.uk/pdbsum/1r48 PDBsum]</span></td></tr>	+	</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=1r48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r48 OCA], [http://pdbe.org/1r48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r48 RCSB], [http://www.ebi.ac.uk/pdbsum/1r48 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 25:		Line 25:
	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 1r48" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:44, 24 December 2014

2014-12-24T15:44:25Z

←Older revision		Revision as of 15:44, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R48 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R48 FirstGlance]. <br>
-	</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=1r48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1r48 RCSB], [http://www.ebi.ac.uk/pdbsum/1r48 PDBsum]</span></td></tr>	+	</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=1r48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1r48 RCSB], [http://www.ebi.ac.uk/pdbsum/1r48 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PROP_ECOLI PROP_ECOLI]] Proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 27:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Hodges, R S.]]	+	[[Category: Hodges, R S]]
-	[[Category: Kutateladze, T G.]]	+	[[Category: Kutateladze, T G]]
-	[[Category: Overduin, M J.]]	+	[[Category: Overduin, M J]]
-	[[Category: Tripet, B P.]]	+	[[Category: Tripet, B P]]
-	[[Category: Wood, J M.]]	+	[[Category: Wood, J M]]
-	[[Category: Zoetewey, D L.]]	+	[[Category: Zoetewey, D L]]
	[[Category: Antiparallel]]		[[Category: Antiparallel]]
	[[Category: Coiled-coil]]		[[Category: Coiled-coil]]

OCA at 16:43, 29 September 2014

2014-09-29T16:43:44Z

←Older revision		Revision as of 16:43, 29 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1r48.~~png\|left~~\|200px]]	+	==Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP==
		+	<StructureSection load='1r48' size='340' side='right' caption='[[1r48]], [[NMR_Ensembles_of_Models \| 51 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R48 FirstGlance]. <br>
		+	</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=1r48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1r48 RCSB], [http://www.ebi.ac.uk/pdbsum/1r48 PDBsum]</span></td></tr>
		+	<table>
		+	== 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/r4/1r48_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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Bacteria respond to increasing medium osmolality by accumulating organic solutes that are compatible with cellular functions. Transporter ProP of Escherichia coli, a proton symporter and a member of the major facilitator superfamily, senses osmotic shifts and responds by importing osmolytes such as glycine betaine. ProP contains a cytoplasmic, C-terminal extension that is essential for its activity. A peptide corresponding to the C-terminal extension of ProP forms a homodimeric alpha-helical coiled-coil even though some of its heptad a positions are not occupied by hydrophobic amino acid residues. Unexpectedly, amino acid replacement R488I, occurring at a heptad a position, destabilized the coiled-coil formed by the ProP peptide and attenuated the response of the intact transporter to osmotic upshifts in vivo. Thus, ProP was proposed to dimerize via an antiparallel coiled-coil. We used nuclear magnetic resonance (NMR) spectroscopy to determine the structure of the synthetic peptide corresponding to residues 468-497 of ProP. This region did form an antiparallel coil-coil in which critical residue R488 specifies the antiparallel coiled-coil orientation by forming stabilizing salt-bridges. Charged residues (both acidic and basic) are clustered on the c/g surface of the coiled-coil whereas polar residues are distributed on the b/e surface. This causes the structure to be bent, in contrast to other known antiparallel coiled-coils (those from the hepatitis delta antigen (PDB ID code 1A92) and the bovine F(1) ATPase inhibitor protein (PDB ID code 1HF9)). The coiled-coil and its possible importance for osmosensing are discussed.

-	~~{{STRUCTURE_1r48\| PDB=1r48 \| SCENE= }}~~	+	Solution structure of the C-terminal antiparallel coiled-coil domain from Escherichia coli osmosensor ProP.,Zoetewey DL, Tripet BP, Kutateladze TG, Overduin MJ, Wood JM, Hodges RS J Mol Biol. 2003 Dec 12;334(5):1063-76. PMID:14643666<ref>PMID:14643666</ref>

-	~~===Solution structure~~ of the ~~C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_14643666}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1r48]] is a 2 chain structure~~. ~~Full experimental information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=1R48 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:014643666<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Hodges, R S.]]		[[Category: Hodges, R S.]]
	[[Category: Kutateladze, T G.]]		[[Category: Kutateladze, T G.]]

OCA: Protected "1r48" [edit=sysop:move=sysop]

2013-01-04T10:52:28Z

Protected "1r48" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:52, 4 January 2013