1pch - Revision history

OCA at 08:06, 14 February 2024

OCA — Wed, 14 Feb 2024 08:06:58 GMT

←Older revision		Revision as of 08:06, 14 February 2024
Line 3:		Line 3:
	<StructureSection load='1pch' size='340' side='right'caption='[[1pch]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1pch' size='340' side='right'caption='[[1pch]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1pch]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_27343 Atcc 27343~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PCH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1pch]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycoplasma_capricolum Mycoplasma capricolum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PCH FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.8Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~PTSH ([https~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2095 ATCC 27343])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pch OCA], [https://pdbe.org/1pch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pch RCSB], [https://www.ebi.ac.uk/pdbsum/1pch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pch 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=1pch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pch OCA], [https://pdbe.org/1pch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pch RCSB], [https://www.ebi.ac.uk/pdbsum/1pch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pch ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PTHP_MYCCT PTHP_MYCCT]] 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_MYCCT PTHP_MYCCT] 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]]
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	</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=1pch 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=1pch ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	BACKGROUND: The three-dimensional structures of histidine-containing phosphocarrier protein (HPr), a member of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), have been determined from Gram-negative and Gram-positive bacteria. The structure of HPr reported here for Mycoplasma capricolum is the first protein structure to be determined for this class of organism. Comparative structural studies with the bacterial proteins highlight sequence-structure correlations relevant to proposals about the evolutionary origin of mycoplasmas. RESULTS: The crystal structure of HPr from M. capricolum has been determined and refined at 1.8 A resolution, revealing the same overall fold as that of other HPrs of known structure. However, mycoplasma HPr resembles HPrs from Gram-positive bacteria more closely than those from Gram-negative bacteria. As in HPrs from Bacillus subtilis and Escherichia coli, the phosphoryl group carrier (His15) forms the N-terminal cap of a helix, but in contrast to the other crystal structures, the side chain of the adjacent Arg17 is conformationally disordered. A sulfate ion interacts with Ser46, a residue known to be phosphorylated in a regulatory manner. CONCLUSIONS: The greater degree of structural similarity of the M. capricolum HPr to HPrs from Gram-positive rather than Gram-negative bacteria is consistent with the proposal that mycoplasma evolved from Gram-positive bacteria. The proposal that no major conformational transition is required for phosphorylation of the active-site histidine is reinforced by comparing the crystal structures with and without an anion in the active site. The conformational disorder of the Arg17 side chain suggests that its guanidinium group does not have to form specific interactions with other protein groups before phosphorylation at His15. The association of a sulfate ion with Ser46 serves as a model for HPr(Ser46-P). As there is no evidence of a conformational change accompanying Ser46 phosphorylation, the inhibitory effect of this event may be attributable to altered surface electrostatics.
-
-	Structural evidence for the evolutionary divergence of mycoplasma from gram-positive bacteria: the histidine-containing phosphocarrier protein.,Pieper U, Kapadia G, Zhu PP, Peterkofsky A, Herzberg O Structure. 1995 Aug 15;3(8):781-90. PMID:7582895<ref>PMID:7582895</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1pch" 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 27343]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Herzberg, O~~]]	+	[[Category: Mycoplasma capricolum]]
-	[[Category: ~~Pieper, U~~]]	+	[[Category: Herzberg O]]
-	[[Category: ~~Phosphotransferase~~]]	+	[[Category: Pieper U]]

OCA at 10:47, 19 May 2021

OCA — Wed, 19 May 2021 10:47:47 GMT

←Older revision		Revision as of 10:47, 19 May 2021
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	<StructureSection load='1pch' size='340' side='right'caption='[[1pch]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1pch' size='340' side='right'caption='[[1pch]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1pch]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_27343 Atcc 27343]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1PCH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1pch]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_27343 Atcc 27343]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PCH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PTSH ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2095 ATCC 27343])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PTSH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2095 ATCC 27343])</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=1pch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pch OCA], [~~http~~://pdbe.org/1pch PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1pch RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1pch PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1pch 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=1pch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pch OCA], [https://pdbe.org/1pch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pch RCSB], [https://www.ebi.ac.uk/pdbsum/1pch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pch ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PTHP_MYCCT PTHP_MYCCT]] 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_MYCCT PTHP_MYCCT]] 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 31:		Line 31:

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

OCA at 10:59, 17 July 2019

OCA — Wed, 17 Jul 2019 10:59:01 GMT

←Older revision		Revision as of 10:59, 17 July 2019
Line 1:		Line 1:

	==STRUCTURAL EVIDENCE FOR THE EVOLUTIONARY DIVERGENCE OF MYCOPLASMA FROM GRAM-POSITIVE BACTERIA: THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN==		==STRUCTURAL EVIDENCE FOR THE EVOLUTIONARY DIVERGENCE OF MYCOPLASMA FROM GRAM-POSITIVE BACTERIA: THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN==
-	<StructureSection load='1pch' size='340' side='right' caption='[[1pch]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='1pch' size='340' side='right'caption='[[1pch]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1pch]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27343 Atcc 27343]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PCH FirstGlance]. <br>		<table><tr><td colspan='2'>[[1pch]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27343 Atcc 27343]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PCH FirstGlance]. <br>
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	</div>		</div>
	<div class="pdbe-citations 1pch" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1pch" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Phosphocarrier protein\|Phosphocarrier protein]]
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 27343]]		[[Category: Atcc 27343]]
		+	[[Category: Large Structures]]
	[[Category: Herzberg, O]]		[[Category: Herzberg, O]]
	[[Category: Pieper, U]]		[[Category: Pieper, U]]
	[[Category: Phosphotransferase]]		[[Category: Phosphotransferase]]

OCA at 08:01, 15 February 2018

OCA — Thu, 15 Feb 2018 08:01:19 GMT

←Older revision		Revision as of 08:01, 15 February 2018
Line 1:		Line 1:
		+
	==STRUCTURAL EVIDENCE FOR THE EVOLUTIONARY DIVERGENCE OF MYCOPLASMA FROM GRAM-POSITIVE BACTERIA: THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN==		==STRUCTURAL EVIDENCE FOR THE EVOLUTIONARY DIVERGENCE OF MYCOPLASMA FROM GRAM-POSITIVE BACTERIA: THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN==
	<StructureSection load='1pch' size='340' side='right' caption='[[1pch]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1pch' size='340' side='right' caption='[[1pch]], [[Resolution\|resolution]] 1.80Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PTSH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2095 ATCC 27343])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PTSH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2095 ATCC 27343])</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=1pch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pch OCA], [http://pdbe.org/1pch PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pch RCSB], [http://www.ebi.ac.uk/pdbsum/1pch 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=1pch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pch OCA], [http://pdbe.org/1pch PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pch RCSB], [http://www.ebi.ac.uk/pdbsum/1pch PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pch ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pc/1pch_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pc/1pch_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>
	</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=1pch ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1pch" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1pch" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Phosphocarrier protein HPr\|Phosphocarrier protein HPr]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:40, 11 September 2015

OCA — Fri, 11 Sep 2015 15:40:29 GMT

←Older revision		Revision as of 15:40, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1pch' size='340' side='right' caption='[[1pch]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1pch' size='340' side='right' caption='[[1pch]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1pch]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mycoplasma_capricolum Mycoplasma capricolum~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PCH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1pch]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27343 Atcc 27343]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PCH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PTSH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2095 ~~Mycoplasma capricolum~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PTSH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2095 ATCC 27343])</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=1pch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pch OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pch RCSB], [http://www.ebi.ac.uk/pdbsum/1pch 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=1pch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pch OCA], [http://pdbe.org/1pch PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pch RCSB], [http://www.ebi.ac.uk/pdbsum/1pch PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PTHP_MYCCT PTHP_MYCCT]] 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 25:		Line 27:
	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 1pch" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 32:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Mycoplasma capricolum~~]]	+	[[Category: Atcc 27343]]
	[[Category: Herzberg, O]]		[[Category: Herzberg, O]]
	[[Category: Pieper, U]]		[[Category: Pieper, U]]
	[[Category: Phosphotransferase]]		[[Category: Phosphotransferase]]

OCA at 07:34, 6 January 2015

OCA — Tue, 06 Jan 2015 07:34:07 GMT

←Older revision		Revision as of 07:34, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1pch]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycoplasma_capricolum Mycoplasma capricolum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PCH FirstGlance]. <br>		<table><tr><td colspan='2'>[[1pch]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycoplasma_capricolum Mycoplasma capricolum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PCH FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PTSH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2095 Mycoplasma capricolum])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PTSH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2095 Mycoplasma capricolum])</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=1pch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pch OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pch RCSB], [http://www.ebi.ac.uk/pdbsum/1pch 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=1pch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pch OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pch RCSB], [http://www.ebi.ac.uk/pdbsum/1pch PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Mycoplasma capricolum]]		[[Category: Mycoplasma capricolum]]
-	[[Category: Herzberg, O.]]	+	[[Category: Herzberg, O]]
-	[[Category: Pieper, U.]]	+	[[Category: Pieper, U]]
	[[Category: Phosphotransferase]]		[[Category: Phosphotransferase]]

OCA at 23:39, 28 September 2014

OCA — Sun, 28 Sep 2014 23:39:07 GMT

←Older revision		Revision as of 23:39, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1pch.~~png~~\|~~left~~\|200px]]	+	==STRUCTURAL EVIDENCE FOR THE EVOLUTIONARY DIVERGENCE OF MYCOPLASMA FROM GRAM-POSITIVE BACTERIA: THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN==
		+	<StructureSection load='1pch' size='340' side='right' caption='[[1pch]], [[Resolution\|resolution]] 1.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1pch]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycoplasma_capricolum Mycoplasma capricolum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PCH FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PTSH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2095 Mycoplasma capricolum])</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=1pch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pch OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pch RCSB], [http://www.ebi.ac.uk/pdbsum/1pch 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/pc/1pch_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 ==
		+	BACKGROUND: The three-dimensional structures of histidine-containing phosphocarrier protein (HPr), a member of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), have been determined from Gram-negative and Gram-positive bacteria. The structure of HPr reported here for Mycoplasma capricolum is the first protein structure to be determined for this class of organism. Comparative structural studies with the bacterial proteins highlight sequence-structure correlations relevant to proposals about the evolutionary origin of mycoplasmas. RESULTS: The crystal structure of HPr from M. capricolum has been determined and refined at 1.8 A resolution, revealing the same overall fold as that of other HPrs of known structure. However, mycoplasma HPr resembles HPrs from Gram-positive bacteria more closely than those from Gram-negative bacteria. As in HPrs from Bacillus subtilis and Escherichia coli, the phosphoryl group carrier (His15) forms the N-terminal cap of a helix, but in contrast to the other crystal structures, the side chain of the adjacent Arg17 is conformationally disordered. A sulfate ion interacts with Ser46, a residue known to be phosphorylated in a regulatory manner. CONCLUSIONS: The greater degree of structural similarity of the M. capricolum HPr to HPrs from Gram-positive rather than Gram-negative bacteria is consistent with the proposal that mycoplasma evolved from Gram-positive bacteria. The proposal that no major conformational transition is required for phosphorylation of the active-site histidine is reinforced by comparing the crystal structures with and without an anion in the active site. The conformational disorder of the Arg17 side chain suggests that its guanidinium group does not have to form specific interactions with other protein groups before phosphorylation at His15. The association of a sulfate ion with Ser46 serves as a model for HPr(Ser46-P). As there is no evidence of a conformational change accompanying Ser46 phosphorylation, the inhibitory effect of this event may be attributable to altered surface electrostatics.

-	~~{{STRUCTURE_1pch\| PDB=1pch \| SCENE= }}~~	+	Structural evidence for the evolutionary divergence of mycoplasma from gram-positive bacteria: the histidine-containing phosphocarrier protein.,Pieper U, Kapadia G, Zhu PP, Peterkofsky A, Herzberg O Structure. 1995 Aug 15;3(8):781-90. PMID:7582895<ref>PMID:7582895</ref>

-	~~===STRUCTURAL EVIDENCE FOR THE EVOLUTIONARY DIVERGENCE OF MYCOPLASMA FROM GRAM-POSITIVE BACTERIA: THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_7582895}}~~	+	==See Also==
-		+	*[[Phosphocarrier protein HPr\|Phosphocarrier protein HPr]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1pch~~]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycoplasma_capricolum Mycoplasma capricolum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:007582895<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Mycoplasma capricolum]]		[[Category: Mycoplasma capricolum]]
	[[Category: Herzberg, O.]]		[[Category: Herzberg, O.]]
	[[Category: Pieper, U.]]		[[Category: Pieper, U.]]
	[[Category: Phosphotransferase]]		[[Category: Phosphotransferase]]

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

OCA — Wed, 19 Dec 2012 12:11:01 GMT

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

←Older revision

Revision as of 12:11, 19 December 2012

OCA at 12:10, 19 December 2012

OCA — Wed, 19 Dec 2012 12:10:58 GMT

←Older revision		Revision as of 12:10, 19 December 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1pch.png\|left\|200px]]		[[Image:1pch.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1pch", 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_1pch\| PDB=1pch \| SCENE= }}		{{STRUCTURE_1pch\| PDB=1pch \| SCENE= }}

	===STRUCTURAL EVIDENCE FOR THE EVOLUTIONARY DIVERGENCE OF MYCOPLASMA FROM GRAM-POSITIVE BACTERIA: THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN===		===STRUCTURAL EVIDENCE FOR THE EVOLUTIONARY DIVERGENCE OF MYCOPLASMA FROM GRAM-POSITIVE BACTERIA: THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_7582895}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 7582895 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_7582895}}		{{ABSTRACT_PUBMED_7582895}}

	==About this Structure==		==About this Structure==
-	~~1PCH~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_capricolum Mycoplasma capricolum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA].	+	[[1pch]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycoplasma_capricolum Mycoplasma capricolum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~7582895~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:007582895</ref><references group="xtra"/>
	[[Category: Mycoplasma capricolum]]		[[Category: Mycoplasma capricolum]]
	[[Category: Herzberg, O.]]		[[Category: Herzberg, O.]]
	[[Category: Pieper, U.]]		[[Category: Pieper, U.]]
	[[Category: Phosphotransferase]]		[[Category: Phosphotransferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:33:11 2009''

OCA at 00:33, 18 February 2009

OCA — Wed, 18 Feb 2009 00:33:13 GMT

←Older revision		Revision as of 00:33, 18 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	1PCH is a ~~[[Single protein]]~~ structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_capricolum Mycoplasma capricolum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA].	+	1PCH is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_capricolum Mycoplasma capricolum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCH OCA].

	==Reference==		==Reference==
-	Structural evidence for the evolutionary divergence of mycoplasma from gram-positive bacteria: the histidine-containing phosphocarrier protein., Pieper U, Kapadia G, Zhu PP, Peterkofsky A, Herzberg O, Structure. 1995 Aug 15;3(8):781-90. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/7582895 7582895]~~	+	<ref group="xtra">PMID:7582895</ref><references group="xtra"/>
	[[Category: Mycoplasma capricolum]]		[[Category: Mycoplasma capricolum]]
-	[[Category: Single protein]]
	[[Category: Herzberg, O.]]		[[Category: Herzberg, O.]]
	[[Category: Pieper, U.]]		[[Category: Pieper, U.]]
	[[Category: Phosphotransferase]]		[[Category: Phosphotransferase]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jul 29 09~~:10:~~38 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:33:11 2009''