1txe - Revision history

OCA at 18:16, 29 May 2024

OCA — Wed, 29 May 2024 18:16:40 GMT

←Older revision		Revision as of 18:16, 29 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=1txe 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=1txe ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	High-pressure NMR experiments performed on the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus have shown that residue Ile14, which is located in the active-centre loop, exhibits a peculiarly small pressure response. In contrast, the rest of the loop shows strong pressure effects as is expected for typical protein interaction sites. To elucidate the structural role of this residue, the mutant protein HPr(I14A), in which Ile14 is replaced by Ala, was produced and studied by solution NMR spectroscopy. On the basis of 1406 structural restraints including 20 directly detected hydrogen bonds, 49 1H(N)-15N, and 25 1H(N)-1Halpha residual dipolar couplings, a well resolved three-dimensional structure could be determined. The overall fold of the protein is not influenced by the mutation but characteristic conformational changes are introduced into the active-centre loop. They lead to a displacement of the ring system of His15 and a distortion of the N-terminus of the first helix, which supports the histidine ring. In addition, the C-terminal helix is bent because the side chain of Leu86 located at the end of this helix partly fills the hydrophobic cavity created by the mutation. Xenon, which is known to occupy hydrophobic cavities, causes a partial reversal of the mutation-induced structural effects. The observed structural changes explain the reduced phosphocarrier activity of the mutant and agree well with the earlier suggestion that Ile14 represents an anchoring point stabilizing the active-centre loop in its correct conformation.
		+
		+	Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphylococcus carnosus.,Moglich A, Koch B, Gronwald W, Hengstenberg W, Brunner E, Kalbitzer HR Eur J Biochem. 2004 Dec;271(23-24):4815-24. PMID:15606769<ref>PMID:15606769</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1txe" style="background-color:#fffaf0;"></div>

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

OCA at 08:45, 1 May 2024

OCA — Wed, 01 May 2024 08:45:14 GMT

←Older revision		Revision as of 08:45, 1 May 2024
Line 1:		Line 1:

	==Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus==		==Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus==
-	<StructureSection load='1txe' size='340' side='right'caption='[[1txe~~]], [[NMR_Ensembles_of_Models \| 10 NMR models~~]]' scene=''>	+	<StructureSection load='1txe' size='340' side='right'caption='[[1txe]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_51365 Atcc 51365~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TXE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_carnosus Staphylococcus carnosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TXE 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;'>[[1qr5\|1qr5]]</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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [https://pdbe.org/1txe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [https://www.ebi.ac.uk/pdbsum/1txe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1txe 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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [https://pdbe.org/1txe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [https://www.ebi.ac.uk/pdbsum/1txe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1txe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PTHP_STACA PTHP_STACA]] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III). P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity).	+	[https://www.uniprot.org/uniprot/PTHP_STACA PTHP_STACA] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III). P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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=1txe 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=1txe ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	High-pressure NMR experiments performed on the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus have shown that residue Ile14, which is located in the active-centre loop, exhibits a peculiarly small pressure response. In contrast, the rest of the loop shows strong pressure effects as is expected for typical protein interaction sites. To elucidate the structural role of this residue, the mutant protein HPr(I14A), in which Ile14 is replaced by Ala, was produced and studied by solution NMR spectroscopy. On the basis of 1406 structural restraints including 20 directly detected hydrogen bonds, 49 1H(N)-15N, and 25 1H(N)-1Halpha residual dipolar couplings, a well resolved three-dimensional structure could be determined. The overall fold of the protein is not influenced by the mutation but characteristic conformational changes are introduced into the active-centre loop. They lead to a displacement of the ring system of His15 and a distortion of the N-terminus of the first helix, which supports the histidine ring. In addition, the C-terminal helix is bent because the side chain of Leu86 located at the end of this helix partly fills the hydrophobic cavity created by the mutation. Xenon, which is known to occupy hydrophobic cavities, causes a partial reversal of the mutation-induced structural effects. The observed structural changes explain the reduced phosphocarrier activity of the mutant and agree well with the earlier suggestion that Ile14 represents an anchoring point stabilizing the active-centre loop in its correct conformation.
-
-	Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphylococcus carnosus.,Moglich A, Koch B, Gronwald W, Hengstenberg W, Brunner E, Kalbitzer HR Eur J Biochem. 2004 Dec;271(23-24):4815-24. PMID:15606769<ref>PMID:15606769</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1txe" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Phosphocarrier protein HPr 3D structures\|Phosphocarrier protein HPr 3D structures]]		*[[Phosphocarrier protein HPr 3D structures\|Phosphocarrier protein HPr 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 51365]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Brunner, E]]	+	[[Category: Staphylococcus carnosus]]
-	[[Category: Hengstenberg, W]]	+	[[Category: Brunner E]]
-	[[Category: Kalbitzer~~, H R~~]]	+	[[Category: Hengstenberg W]]
-	[[Category: Koch, B]]	+	[[Category: Kalbitzer HR]]
-	[[Category: Moeglich, A]]	+	[[Category: Koch B]]
-	~~[[Category: SPINE, Structural Proteomics in Europe]]~~	+	[[Category: Moeglich A]]
-	~~[[Category: Open-faced beta-sandwich]]~~	+
-	~~[[Category: Spine]]~~	+
-	~~[[Category: Structural genomic]]~~	+
-	~~[[Category: Structural proteomics in europe]]~~	+
-	~~[[Category: Transport protein~~]]	+

OCA at 09:33, 29 September 2021

OCA — Wed, 29 Sep 2021 09:33:53 GMT

←Older revision		Revision as of 09:33, 29 September 2021
Line 3:		Line 3:
	<StructureSection load='1txe' size='340' side='right'caption='[[1txe]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1txe' size='340' side='right'caption='[[1txe]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_51365 Atcc 51365]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1TXE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_51365 Atcc 51365]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TXE FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qr5\|1qr5]]</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;'>[[1qr5\|1qr5]]</div></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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [~~http~~://pdbe.org/1txe PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1txe PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1txe 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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [https://pdbe.org/1txe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [https://www.ebi.ac.uk/pdbsum/1txe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1txe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PTHP_STACA PTHP_STACA]] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III). P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity).	+	[[https://www.uniprot.org/uniprot/PTHP_STACA PTHP_STACA]] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III). P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 14:10, 25 December 2019

OCA — Wed, 25 Dec 2019 14:10:20 GMT

←Older revision		Revision as of 14:10, 25 December 2019
Line 1:		Line 1:

	==Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus==		==Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus==
-	<StructureSection load='1txe' size='340' side='right' caption='[[1txe]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>	+	<StructureSection load='1txe' size='340' side='right'caption='[[1txe]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51365 Atcc 51365]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TXE FirstGlance]. <br>		<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51365 Atcc 51365]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TXE FirstGlance]. <br>
Line 30:		Line 30:

	==See Also==		==See Also==
-	*[[Phosphocarrier protein\|Phosphocarrier protein]]	+	*[[Phosphocarrier protein HPr 3D structures\|Phosphocarrier protein HPr 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 51365]]		[[Category: Atcc 51365]]
		+	[[Category: Large Structures]]
	[[Category: Brunner, E]]		[[Category: Brunner, E]]
	[[Category: Hengstenberg, W]]		[[Category: Hengstenberg, W]]

OCA at 08:59, 21 March 2018

OCA — Wed, 21 Mar 2018 08:59:23 GMT

←Older revision		Revision as of 08:59, 21 March 2018
Line 1:		Line 1:
		+
	==Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus==		==Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus==
	<StructureSection load='1txe' size='340' side='right' caption='[[1txe]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1txe' size='340' side='right' caption='[[1txe]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51365 Atcc 51365]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TXE FirstGlance]. <br>		<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51365 Atcc 51365]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TXE FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qr5\|1qr5]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qr5\|1qr5]]</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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [http://pdbe.org/1txe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [http://www.ebi.ac.uk/pdbsum/1txe 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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [http://pdbe.org/1txe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [http://www.ebi.ac.uk/pdbsum/1txe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1txe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tx/1txe_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tx/1txe_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>
Line 29:		Line 30:

	==See Also==		==See Also==
-	*[[Phosphocarrier protein ~~HPr~~\|Phosphocarrier protein ~~HPr~~]]	+	*[[Phosphocarrier protein\|Phosphocarrier protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 22:29, 8 February 2016

OCA — Mon, 08 Feb 2016 22:29:18 GMT

←Older revision		Revision as of 22:29, 8 February 2016
Line 16:		Line 16:
	<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=1txe ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 15:58, 10 September 2015

OCA — Thu, 10 Sep 2015 15:58:02 GMT

←Older revision		Revision as of 15:58, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1txe' size='340' side='right' caption='[[1txe]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1txe' size='340' side='right' caption='[[1txe]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Staphylococcus_carnosus Staphylococcus carnosus~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TXE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51365 Atcc 51365]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TXE FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qr5\|1qr5]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qr5\|1qr5]]</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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [http://www.ebi.ac.uk/pdbsum/1txe 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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [http://pdbe.org/1txe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [http://www.ebi.ac.uk/pdbsum/1txe PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 26:
	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 1txe" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Staphylococcus carnosus~~]]	+	[[Category: Atcc 51365]]
	[[Category: Brunner, E]]		[[Category: Brunner, E]]
	[[Category: Hengstenberg, W]]		[[Category: Hengstenberg, W]]

OCA at 02:33, 25 December 2014

OCA — Thu, 25 Dec 2014 02:33:46 GMT

←Older revision		Revision as of 02:33, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_carnosus Staphylococcus carnosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TXE FirstGlance]. <br>		<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_carnosus Staphylococcus carnosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TXE FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qr5\|1qr5]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qr5\|1qr5]]</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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [http://www.ebi.ac.uk/pdbsum/1txe 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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [http://www.ebi.ac.uk/pdbsum/1txe PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PTHP_STACA PTHP_STACA]] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III). P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Staphylococcus carnosus]]		[[Category: Staphylococcus carnosus]]
-	[[Category: Brunner, E.]]	+	[[Category: Brunner, E]]
-	[[Category: Hengstenberg, W.]]	+	[[Category: Hengstenberg, W]]
-	[[Category: Kalbitzer, H R.]]	+	[[Category: Kalbitzer, H R]]
-	[[Category: Koch, B.]]	+	[[Category: Koch, B]]
-	[[Category: Moeglich, A.]]	+	[[Category: Moeglich, A]]
-	[[Category: SPINE, Structural Proteomics in Europe.]]	+	[[Category: SPINE, Structural Proteomics in Europe]]
	[[Category: Open-faced beta-sandwich]]		[[Category: Open-faced beta-sandwich]]
	[[Category: Spine]]		[[Category: Spine]]

OCA at 22:03, 29 September 2014

OCA — Mon, 29 Sep 2014 22:03:31 GMT

←Older revision		Revision as of 22:03, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1txe.~~png~~\|~~left~~\|200px]]	+	==Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus==
		+	<StructureSection load='1txe' size='340' side='right' caption='[[1txe]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_carnosus Staphylococcus carnosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TXE FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qr5\|1qr5]]</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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [http://www.ebi.ac.uk/pdbsum/1txe 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/tx/1txe_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 ==
		+	High-pressure NMR experiments performed on the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus have shown that residue Ile14, which is located in the active-centre loop, exhibits a peculiarly small pressure response. In contrast, the rest of the loop shows strong pressure effects as is expected for typical protein interaction sites. To elucidate the structural role of this residue, the mutant protein HPr(I14A), in which Ile14 is replaced by Ala, was produced and studied by solution NMR spectroscopy. On the basis of 1406 structural restraints including 20 directly detected hydrogen bonds, 49 1H(N)-15N, and 25 1H(N)-1Halpha residual dipolar couplings, a well resolved three-dimensional structure could be determined. The overall fold of the protein is not influenced by the mutation but characteristic conformational changes are introduced into the active-centre loop. They lead to a displacement of the ring system of His15 and a distortion of the N-terminus of the first helix, which supports the histidine ring. In addition, the C-terminal helix is bent because the side chain of Leu86 located at the end of this helix partly fills the hydrophobic cavity created by the mutation. Xenon, which is known to occupy hydrophobic cavities, causes a partial reversal of the mutation-induced structural effects. The observed structural changes explain the reduced phosphocarrier activity of the mutant and agree well with the earlier suggestion that Ile14 represents an anchoring point stabilizing the active-centre loop in its correct conformation.

-	~~{{STRUCTURE_1txe\| PDB=1txe \| SCENE= }}~~	+	Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphylococcus carnosus.,Moglich A, Koch B, Gronwald W, Hengstenberg W, Brunner E, Kalbitzer HR Eur J Biochem. 2004 Dec;271(23-24):4815-24. PMID:15606769<ref>PMID:15606769</ref>

-	~~===Solution structure~~ of the ~~active-centre mutant Ile14Ala~~ of ~~the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_15606769}}~~	+	==See Also==
-		+	*[[Phosphocarrier protein HPr\|Phosphocarrier protein HPr]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1txe~~]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_carnosus Staphylococcus carnosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:015606769<~~/~~ref~~><~~ref group="xtra">PMID:010794411</ref><ref group="xtra">PMID:012862458</ref><ref group="xtra">PMID:015103611</ref><ref group="xtra">PMID:012557191</ref><references group="xtra"~~/>	+
	[[Category: Staphylococcus carnosus]]		[[Category: Staphylococcus carnosus]]
	[[Category: Brunner, E.]]		[[Category: Brunner, E.]]

OCA at 09:44, 16 January 2013

OCA — Wed, 16 Jan 2013 09:44:39 GMT

←Older revision		Revision as of 09:44, 16 January 2013
Line 1:		Line 1:
	[[Image:1txe.png\|left\|200px]]		[[Image:1txe.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1txe", 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.
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	{{STRUCTURE_1txe\| PDB=1txe \| SCENE= }}		{{STRUCTURE_1txe\| PDB=1txe \| SCENE= }}

	===Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus===		===Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15606769}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15606769 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_15606769}}		{{ABSTRACT_PUBMED_15606769}}

Line 22:		Line 11:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15606769~~</ref><ref group="xtra">PMID:~~10794411~~</ref><ref group="xtra">PMID:~~12862458~~</ref><ref group="xtra">PMID:~~15103611~~</ref><ref group="xtra">PMID:~~12557191~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015606769</ref><ref group="xtra">PMID:010794411</ref><ref group="xtra">PMID:012862458</ref><ref group="xtra">PMID:015103611</ref><ref group="xtra">PMID:012557191</ref><references group="xtra"/>
	[[Category: Staphylococcus carnosus]]		[[Category: Staphylococcus carnosus]]
	[[Category: Brunner, E.]]		[[Category: Brunner, E.]]