1jde - Revision history

OCA at 07:38, 7 February 2024

OCA — Wed, 07 Feb 2024 07:38:49 GMT

←Older revision		Revision as of 07:38, 7 February 2024
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	<StructureSection load='1jde' size='340' side='right'caption='[[1jde]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1jde' size='340' side='right'caption='[[1jde]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1jde]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacteroides_symbiosus"_stevens_1956 "bacteroides symbiosus" stevens 1956~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JDE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1jde]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JDE 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]] 2.8Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max~~-~~height: 3em;'>[[1dik\|1dik]]~~, [[~~2dik~~\|~~2dik]], [[1ggo\|1ggo~~]]~~</div>~~</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"~~>PODK ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~1512~~ "~~Bacteroides symbiosus~~" ~~Stevens 1956])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1]~~ </~~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=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [https://pdbe.org/1jde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [https://www.ebi.ac.uk/pdbsum/1jde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jde 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=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [https://pdbe.org/1jde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [https://www.ebi.ac.uk/pdbsum/1jde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jde ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PPDK_CLOSY PPDK_CLOSY]] Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis.	+	[https://www.uniprot.org/uniprot/PPDK_CLOSY PPDK_CLOSY] Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis.
	== 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=1jde 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=1jde ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Pyruvate phosphate dikinase (PPDK) catalyzes the interconversion of ATP, P(i), and pyruvate with AMP, PP(i), and phosphoenolpyruvate (PEP) in three partial reactions as follows: 1) E-His + ATP --> E-His-PP.AMP; 2) E-His-PP.AMP + P(i) --> E-His-P.AMP.PP(i); and 3) E-His-P + pyruvate --> E.PEP using His-455 as the carrier of the transferred phosphoryl groups. The crystal structure of the Clostridium symbiosum PPDK (in the unbound state) reveals a three-domain structure consisting of consecutive N-terminal, central His-455, and C-terminal domains. The N-terminal and central His-455 domains catalyze partial reactions 1 and 2, whereas the C-terminal and central His-455 domains catalyze partial reaction 3. Attempts to obtain a crystal structure of the enzyme with substrate ligands bound at the nucleotide binding domain have been unsuccessful. The object of the present study is to demonstrate Mg(II) activation of catalysis at the ATP/P(i) active site, to identify the residues at the ATP/P(i) active site that contribute to catalysis, and to identify roles for these residues based on their positions within the active site scaffold. First, Mg(II) activation studies of catalysis of E + ATP + P(i) --> E-P + AMP + PP(i) partial reaction were carried out using a truncation mutant (Tem533) in which the C-terminal domain is absent. The kinetics show that a minimum of 2 Mg(II) per active site is required for the reaction. The active site residues used for substrate/cofactor binding/activation were identified by site-directed mutagenesis. Lys-22, Arg-92, Asp-321, Glu-323, and Gln-335 mutants were found to be inactive; Arg-337, Glu-279, Asp-280, and Arg-135 mutants were partially active; and Thr-253 and Gln-240 mutants were almost fully active. The participation of the nucleotide ribose 2'-OH and alpha-P in enzyme binding is indicated by the loss of productive binding seen with substrate analogs modified at these positions. The ATP, P(i), and Mg(II) ions were docked into the PPDK N-terminal domain crevice, in an orientation consistent with substrate/cofactor binding modes observed for other members of the ATP-Grasp fold enzyme superfamily and consistent with the structure-function data. On the basis of this docking model, the ATP polyphosphate moiety is oriented/activated for pyrophosphoryl transfer through interaction with Lys-22 (gamma-P), Arg-92 (alpha-P), and the Gly-101 to Met-103 loop (gamma-P) as well as with the Mg(II) cofactors. The P(i) is oriented/activated for partial reaction 2 through interaction with Arg-337 and a Mg(II) cofactor. The Mg(II) ions are bound through interaction with Asp-321, Glu-323, and Gln-335 and substrate. Residues Glu-279, Asp-280, and Arg-135 are suggested to function in the closure of an active site loop, over the nucleotide ribose-binding site.
-
-	Investigation of the catalytic site within the ATP-grasp domain of Clostridium symbiosum pyruvate phosphate dikinase.,Ye D, Wei M, McGuire M, Huang K, Kapadia G, Herzberg O, Martin BM, Dunaway-Mariano D J Biol Chem. 2001 Oct 5;276(40):37630-9. Epub 2001 Jul 23. PMID:11468288<ref>PMID:11468288</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1jde" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Pyruvate phosphate dikinase\|Pyruvate phosphate dikinase]]		*[[Pyruvate phosphate dikinase\|Pyruvate phosphate dikinase]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bacteroides symbiosus stevens 1956]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Pyruvate, phosphate dikinase]]~~	+	[[Category: Dunaway-Mariano D]]
-	[[Category: Dunaway-Mariano, D]]	+	[[Category: Herzberg O]]
-	[[Category: Herzberg, O]]	+	[[Category: Huang K]]
-	[[Category: Huang, K]]	+	[[Category: Kapadia G]]
-	[[Category: Kapadia, G]]	+	[[Category: Martin BM]]
-	[[Category: Martin~~, B M~~]]	+	[[Category: McGuire M]]
-	[[Category: McGuire, M]]	+	[[Category: Wei M]]
-	[[Category: Wei, M]]	+	[[Category: Ye D]]
-	[[Category: Ye, D]]	+
-	~~[[Category: Kinase]]~~	+
-	~~[[Category: Nucleotide binding site mutant]]~~	+
-	~~[[Category: Phosphotransferase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 14:30, 27 October 2021

OCA — Wed, 27 Oct 2021 14:30:26 GMT

OCA at 07:30, 25 November 2020

OCA — Wed, 25 Nov 2020 07:30:16 GMT

←Older revision		Revision as of 07:30, 25 November 2020
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	==K22A mutant of pyruvate, phosphate dikinase==		==K22A mutant of pyruvate, phosphate dikinase==
-	<StructureSection load='1jde' size='340' side='right' caption='[[1jde]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='1jde' size='340' side='right'caption='[[1jde]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1jde]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacteroides_symbiosus"_stevens_1956 "bacteroides symbiosus" stevens 1956]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1JDE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1jde]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacteroides_symbiosus"_stevens_1956 "bacteroides symbiosus" stevens 1956]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JDE 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dik\|1dik]], [[2dik\|2dik]], [[1ggo\|1ggo]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dik\|1dik]], [[2dik\|2dik]], [[1ggo\|1ggo]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PODK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 "Bacteroides symbiosus" Stevens 1956])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PODK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 "Bacteroides symbiosus" Stevens 1956])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </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=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [http://pdbe.org/1jde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [http://www.ebi.ac.uk/pdbsum/1jde PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jde ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [http://pdbe.org/1jde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [http://www.ebi.ac.uk/pdbsum/1jde PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jde ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</StructureSection>		</StructureSection>
	[[Category: Bacteroides symbiosus stevens 1956]]		[[Category: Bacteroides symbiosus stevens 1956]]
		+	[[Category: Large Structures]]
	[[Category: Pyruvate, phosphate dikinase]]		[[Category: Pyruvate, phosphate dikinase]]
	[[Category: Dunaway-Mariano, D]]		[[Category: Dunaway-Mariano, D]]

OCA at 06:15, 4 April 2018

OCA — Wed, 04 Apr 2018 06:15:08 GMT

←Older revision		Revision as of 06:15, 4 April 2018
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	</div>		</div>
	<div class="pdbe-citations 1jde" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1jde" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Pyruvate phosphate dikinase\|Pyruvate phosphate dikinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:41, 17 January 2018

OCA — Wed, 17 Jan 2018 08:41:51 GMT

←Older revision		Revision as of 08:41, 17 January 2018
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		+
	==K22A mutant of pyruvate, phosphate dikinase==		==K22A mutant of pyruvate, phosphate dikinase==
	<StructureSection load='1jde' size='340' side='right' caption='[[1jde]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1jde' size='340' side='right' caption='[[1jde]], [[Resolution\|resolution]] 2.80Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PODK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 "Bacteroides symbiosus" Stevens 1956])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PODK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 "Bacteroides symbiosus" Stevens 1956])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </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=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [http://pdbe.org/1jde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [http://www.ebi.ac.uk/pdbsum/1jde 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=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [http://pdbe.org/1jde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [http://www.ebi.ac.uk/pdbsum/1jde PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jde ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jd/1jde_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jd/1jde_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 30:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1jde" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1jde" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Pyruvate phosphate dikinase\|Pyruvate phosphate dikinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:02, 8 February 2016

OCA — Mon, 08 Feb 2016 02:02:48 GMT

←Older revision		Revision as of 02:02, 8 February 2016
Line 19:		Line 19:
	<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=1jde ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 06:50, 10 September 2015

OCA — Thu, 10 Sep 2015 06:50:14 GMT

←Older revision		Revision as of 06:50, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1jde' size='340' side='right' caption='[[1jde]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1jde' size='340' side='right' caption='[[1jde]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1jde]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Clostridium_symbiosum Clostridium symbiosum~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JDE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1jde]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacteroides_symbiosus"_stevens_1956 "bacteroides symbiosus" stevens 1956]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JDE 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dik\|1dik]], [[2dik\|2dik]], [[1ggo\|1ggo]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dik\|1dik]], [[2dik\|2dik]], [[1ggo\|1ggo]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PODK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 ~~Clostridium symbiosum~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PODK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 "Bacteroides symbiosus" Stevens 1956])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </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=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [http://www.ebi.ac.uk/pdbsum/1jde 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=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [http://pdbe.org/1jde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [http://www.ebi.ac.uk/pdbsum/1jde PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 29:
	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 1jde" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Clostridium symbiosum~~]]	+	[[Category: Bacteroides symbiosus stevens 1956]]
	[[Category: Pyruvate, phosphate dikinase]]		[[Category: Pyruvate, phosphate dikinase]]
	[[Category: Dunaway-Mariano, D]]		[[Category: Dunaway-Mariano, D]]

OCA at 19:45, 24 December 2014

OCA — Wed, 24 Dec 2014 19:45:15 GMT

←Older revision		Revision as of 19:45, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1jde]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JDE FirstGlance]. <br>		<table><tr><td colspan='2'>[[1jde]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JDE 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>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dik\|1dik]], [[2dik\|2dik]], [[1ggo\|1ggo]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dik\|1dik]], [[2dik\|2dik]], [[1ggo\|1ggo]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PODK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 Clostridium symbiosum])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PODK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 Clostridium symbiosum])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [http://www.ebi.ac.uk/pdbsum/1jde 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=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [http://www.ebi.ac.uk/pdbsum/1jde PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PPDK_CLOSY PPDK_CLOSY]] Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Clostridium symbiosum]]		[[Category: Clostridium symbiosum]]
	[[Category: Pyruvate, phosphate dikinase]]		[[Category: Pyruvate, phosphate dikinase]]
-	[[Category: Dunaway-Mariano, D.]]	+	[[Category: Dunaway-Mariano, D]]
-	[[Category: Herzberg, O.]]	+	[[Category: Herzberg, O]]
-	[[Category: Huang, K.]]	+	[[Category: Huang, K]]
-	[[Category: Kapadia, G.]]	+	[[Category: Kapadia, G]]
-	[[Category: Martin, B M.]]	+	[[Category: Martin, B M]]
-	[[Category: McGuire, M.]]	+	[[Category: McGuire, M]]
-	[[Category: Wei, M.]]	+	[[Category: Wei, M]]
-	[[Category: Ye, D.]]	+	[[Category: Ye, D]]
	[[Category: Kinase]]		[[Category: Kinase]]
	[[Category: Nucleotide binding site mutant]]		[[Category: Nucleotide binding site mutant]]
	[[Category: Phosphotransferase]]		[[Category: Phosphotransferase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 11:41, 28 September 2014

OCA — Sun, 28 Sep 2014 11:41:16 GMT

←Older revision		Revision as of 11:41, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1jde.~~png~~\|~~left~~\|200px]]	+	==K22A mutant of pyruvate, phosphate dikinase==
		+	<StructureSection load='1jde' size='340' side='right' caption='[[1jde]], [[Resolution\|resolution]] 2.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1jde]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JDE 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>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dik\|1dik]], [[2dik\|2dik]], [[1ggo\|1ggo]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PODK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 Clostridium symbiosum])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [http://www.ebi.ac.uk/pdbsum/1jde 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/jd/1jde_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 ==
		+	Pyruvate phosphate dikinase (PPDK) catalyzes the interconversion of ATP, P(i), and pyruvate with AMP, PP(i), and phosphoenolpyruvate (PEP) in three partial reactions as follows: 1) E-His + ATP --> E-His-PP.AMP; 2) E-His-PP.AMP + P(i) --> E-His-P.AMP.PP(i); and 3) E-His-P + pyruvate --> E.PEP using His-455 as the carrier of the transferred phosphoryl groups. The crystal structure of the Clostridium symbiosum PPDK (in the unbound state) reveals a three-domain structure consisting of consecutive N-terminal, central His-455, and C-terminal domains. The N-terminal and central His-455 domains catalyze partial reactions 1 and 2, whereas the C-terminal and central His-455 domains catalyze partial reaction 3. Attempts to obtain a crystal structure of the enzyme with substrate ligands bound at the nucleotide binding domain have been unsuccessful. The object of the present study is to demonstrate Mg(II) activation of catalysis at the ATP/P(i) active site, to identify the residues at the ATP/P(i) active site that contribute to catalysis, and to identify roles for these residues based on their positions within the active site scaffold. First, Mg(II) activation studies of catalysis of E + ATP + P(i) --> E-P + AMP + PP(i) partial reaction were carried out using a truncation mutant (Tem533) in which the C-terminal domain is absent. The kinetics show that a minimum of 2 Mg(II) per active site is required for the reaction. The active site residues used for substrate/cofactor binding/activation were identified by site-directed mutagenesis. Lys-22, Arg-92, Asp-321, Glu-323, and Gln-335 mutants were found to be inactive; Arg-337, Glu-279, Asp-280, and Arg-135 mutants were partially active; and Thr-253 and Gln-240 mutants were almost fully active. The participation of the nucleotide ribose 2'-OH and alpha-P in enzyme binding is indicated by the loss of productive binding seen with substrate analogs modified at these positions. The ATP, P(i), and Mg(II) ions were docked into the PPDK N-terminal domain crevice, in an orientation consistent with substrate/cofactor binding modes observed for other members of the ATP-Grasp fold enzyme superfamily and consistent with the structure-function data. On the basis of this docking model, the ATP polyphosphate moiety is oriented/activated for pyrophosphoryl transfer through interaction with Lys-22 (gamma-P), Arg-92 (alpha-P), and the Gly-101 to Met-103 loop (gamma-P) as well as with the Mg(II) cofactors. The P(i) is oriented/activated for partial reaction 2 through interaction with Arg-337 and a Mg(II) cofactor. The Mg(II) ions are bound through interaction with Asp-321, Glu-323, and Gln-335 and substrate. Residues Glu-279, Asp-280, and Arg-135 are suggested to function in the closure of an active site loop, over the nucleotide ribose-binding site.

-	~~{{STRUCTURE_1jde\| PDB=1jde \| SCENE= }}~~	+	Investigation of the catalytic site within the ATP-grasp domain of Clostridium symbiosum pyruvate phosphate dikinase.,Ye D, Wei M, McGuire M, Huang K, Kapadia G, Herzberg O, Martin BM, Dunaway-Mariano D J Biol Chem. 2001 Oct 5;276(40):37630-9. Epub 2001 Jul 23. PMID:11468288<ref>PMID:11468288</ref>

-	~~===K22A mutant of pyruvate~~, ~~phosphate dikinase===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11468288}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1jde]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Clostridium_symbiosum Clostridium symbiosum]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA].~~	+

	==See Also==		==See Also==
	*[[Pyruvate phosphate dikinase\|Pyruvate phosphate dikinase]]		*[[Pyruvate phosphate dikinase\|Pyruvate phosphate dikinase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:011468288<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Clostridium symbiosum]]		[[Category: Clostridium symbiosum]]
	[[Category: Pyruvate, phosphate dikinase]]		[[Category: Pyruvate, phosphate dikinase]]

OCA at 08:32, 20 October 2012

OCA — Sat, 20 Oct 2012 08:32:04 GMT

←Older revision		Revision as of 08:32, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1jde]] is a 1 chain structure ~~of [[Pyruvate phosphate dikinase]]~~ with sequence from [http://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA].	+	[[1jde]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA].

	==See Also==		==See Also==

←Older revision		Revision as of 14:30, 27 October 2021
Line 3:		Line 3:
	<StructureSection load='1jde' size='340' side='right'caption='[[1jde]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1jde' size='340' side='right'caption='[[1jde]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1jde]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacteroides_symbiosus"_stevens_1956 "bacteroides symbiosus" stevens 1956]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1JDE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1jde]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacteroides_symbiosus"_stevens_1956 "bacteroides symbiosus" stevens 1956]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JDE 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='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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dik\|1dik]], [[2dik\|2dik]], [[1ggo\|1ggo]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dik\|1dik]], [[2dik\|2dik]], [[1ggo\|1ggo]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PODK ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 "Bacteroides symbiosus" Stevens 1956])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PODK ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 "Bacteroides symbiosus" Stevens 1956])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [~~http~~://pdbe.org/1jde PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1jde PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1jde 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=1jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jde OCA], [https://pdbe.org/1jde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jde RCSB], [https://www.ebi.ac.uk/pdbsum/1jde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jde ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PPDK_CLOSY PPDK_CLOSY]] Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis.	+	[[https://www.uniprot.org/uniprot/PPDK_CLOSY PPDK_CLOSY]] Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]