3l8e - Revision history

OCA at 10:19, 21 February 2024

OCA — Wed, 21 Feb 2024 10:19:33 GMT

←Older revision		Revision as of 10:19, 21 February 2024
Line 1:		Line 1:

	==Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli==		==Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli==
-	<StructureSection load='3l8e' size='340' side='right' caption='[[3l8e]], [[Resolution\|resolution]] 1.64Å' scene=''>	+	<StructureSection load='3l8e' size='340' side='right'caption='[[3l8e]], [[Resolution\|resolution]] 1.64Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3l8e]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L8E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3L8E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3l8e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L8E FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=ACY:ACETIC+ACID'>ACY</scene~~>, ~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.64Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[3l8f\|3l8f]], [[3l8g\|3l8g]], [[3l8h\|3l8h]]~~<~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<~~tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">b0200, gmhB, JW0196, yaeD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])~~</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=3l8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l8e OCA], [https://pdbe.org/3l8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l8e RCSB], [https://www.ebi.ac.uk/pdbsum/3l8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l8e ProSAT]</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=3l8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l8e OCA], [~~http~~://pdbe.org/3l8e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3l8e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3l8e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3l8e ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~GMHB_ECOLI GMHB_ECOLI]~~] Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate ~~(HBP)~~ by removing the phosphate group at the C-7 position~~. Also catalyzes the dephosphorylation of fructose-1,6-bisphosphate (Fru1,6bisP)~~.<ref>PMID:11751812</ref> <ref>PMID:16990279</ref>	+	[https://www.uniprot.org/uniprot/GMHBB_ECOLI GMHBB_ECOLI] Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.<ref>PMID:11751812</ref> <ref>PMID:16990279</ref> <ref>PMID:20050615</ref> <ref>PMID:31449400</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l8/3l8e_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l8/3l8e_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 21:		Line 20:
	</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=3l8e 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=3l8e ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The haloalkanoic acid dehalogenase (HAD) enzyme superfamily is the largest family of phosphohydrolases. In HAD members, the structural elements that provide the binding interactions that support substrate specificity are separated from those that orchestrate catalysis. For most HAD phosphatases, a cap domain functions in substrate recognition. However, for the HAD phosphatases that lack a cap domain, an alternate strategy for substrate selection must be operative. One such HAD phosphatase, GmhB of the HisB subfamily, was selected for structure-function analysis. Herein, the X-ray crystallographic structures of Escherichia coli GmhB in the apo form (1.6 A resolution), in a complex with Mg(2+) and orthophosphate (1.8 A resolution), and in a complex with Mg(2+) and d-glycero-d-manno-heptose 1beta,7-bisphosphate (2.2 A resolution) were determined, in addition to the structure of Bordetella bronchiseptica GmhB bound to Mg(2+) and orthophosphate (1.7 A resolution). The structures show that in place of a cap domain, the GmhB catalytic site is elaborated by three peptide inserts or loops that pack to form a concave, semicircular surface around the substrate leaving group. Structure-guided kinetic analysis of site-directed mutants was conducted in parallel with a bioinformatics study of sequence diversification within the HisB subfamily to identify loop residues that serve as substrate recognition elements and that distinguish GmhB from its subfamily counterpart, the histidinol-phosphate phosphatase domain of HisB. We show that GmhB and the histidinol-phosphate phosphatase domain use the same design of three substrate recognition loops inserted into the cap domain yet, through selective residue usage on the loops, have achieved unique substrate specificity and thus novel biochemical function.
-
-	Structural Determinants of Substrate Recognition in the HAD Superfamily Member d-glycero-d-manno-Heptose-1,7-bisphosphate Phosphatase (GmhB) .,Nguyen HH, Wang L, Huang H, Peisach E, Dunaway-Mariano D, Allen KN Biochemistry. 2010 Jan 22. PMID:20050614<ref>PMID:20050614</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3l8e" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli]]~~	+	[[Category: Escherichia coli K-12]]
-	~~[[Category: Allen,~~ K ~~N]]~~	+	[[Category: Large Structures]]
-	~~[[Category: Nguyen, H]]~~	+	[[Category: Allen KN]]
-	~~[[Category: Peisach, E]]~~	+	[[Category: Nguyen H]]
-	~~[[Category: 7~~-~~bisphosphate phosphatase~~]]	+	[[Category: Peisach E]]
-	[[Category: ~~Carbohydrate metabolism~~]]	+
-	[[Category: ~~Cytoplasm~~]]	+
-	[[Category: ~~D-glycero-d-manno-heptose-1~~]]	+
-	[[Category: ~~Gmhb]]~~	+
-	~~[[Category: Had superfamily]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Lipopolysaccharide biosynthesis~~]]	+

OCA at 08:50, 1 November 2017

OCA — Wed, 01 Nov 2017 08:50:46 GMT

←Older revision		Revision as of 08:50, 1 November 2017
Line 40:		Line 40:
	[[Category: 7-bisphosphate phosphatase]]		[[Category: 7-bisphosphate phosphatase]]
	[[Category: Carbohydrate metabolism]]		[[Category: Carbohydrate metabolism]]
		+	[[Category: Cytoplasm]]
	[[Category: D-glycero-d-manno-heptose-1]]		[[Category: D-glycero-d-manno-heptose-1]]
	[[Category: Gmhb]]		[[Category: Gmhb]]

OCA at 23:06, 5 August 2016

OCA — Fri, 05 Aug 2016 23:06:19 GMT

←Older revision		Revision as of 23:06, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli==		==Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli==
	<StructureSection load='3l8e' size='340' side='right' caption='[[3l8e]], [[Resolution\|resolution]] 1.64Å' scene=''>		<StructureSection load='3l8e' size='340' side='right' caption='[[3l8e]], [[Resolution\|resolution]] 1.64Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3l8e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia coli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L8E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3l8e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L8E FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l8f\|3l8f]], [[3l8g\|3l8g]], [[3l8h\|3l8h]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l8f\|3l8f]], [[3l8g\|3l8g]], [[3l8h\|3l8h]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0200, gmhB, JW0196, yaeD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~562 Escherichia coli~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0200, gmhB, JW0196, yaeD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3l8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l8e RCSB], [http://www.ebi.ac.uk/pdbsum/3l8e 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=3l8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l8e OCA], [http://pdbe.org/3l8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l8e RCSB], [http://www.ebi.ac.uk/pdbsum/3l8e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l8e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		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=3l8e 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:
	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 3l8e" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli~~]]	+	[[Category: Ecoli]]
	[[Category: Allen, K N]]		[[Category: Allen, K N]]
	[[Category: Nguyen, H]]		[[Category: Nguyen, H]]

OCA at 22:43, 25 December 2014

OCA — Thu, 25 Dec 2014 22:43:43 GMT

←Older revision		Revision as of 22:43, 25 December 2014
Line 8:		Line 8:
	<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=3l8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l8e RCSB], [http://www.ebi.ac.uk/pdbsum/3l8e 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=3l8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l8e RCSB], [http://www.ebi.ac.uk/pdbsum/3l8e PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GMHB_ECOLI GMHB_ECOLI]] Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate (HBP) by removing the phosphate group at the C-7 position. Also catalyzes the dephosphorylation of fructose-1,6-bisphosphate (Fru1,6bisP).<ref>PMID:11751812</ref> <ref>PMID:16990279</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 17:49, 18 December 2014

OCA — Thu, 18 Dec 2014 17:49:23 GMT

←Older revision		Revision as of 17:49, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3l8e\| PDB=3l8e \| SCENE= }}~~	+	==Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli==
-	===Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli===	+	<StructureSection load='3l8e' size='340' side='right' caption='[[3l8e]], [[Resolution\|resolution]] 1.64Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20050614}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3l8e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L8E FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l8f\|3l8f]], [[3l8g\|3l8g]], [[3l8h\|3l8h]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0200, gmhB, JW0196, yaeD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3l8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l8e RCSB], [http://www.ebi.ac.uk/pdbsum/3l8e 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/l8/3l8e_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 ==
		+	The haloalkanoic acid dehalogenase (HAD) enzyme superfamily is the largest family of phosphohydrolases. In HAD members, the structural elements that provide the binding interactions that support substrate specificity are separated from those that orchestrate catalysis. For most HAD phosphatases, a cap domain functions in substrate recognition. However, for the HAD phosphatases that lack a cap domain, an alternate strategy for substrate selection must be operative. One such HAD phosphatase, GmhB of the HisB subfamily, was selected for structure-function analysis. Herein, the X-ray crystallographic structures of Escherichia coli GmhB in the apo form (1.6 A resolution), in a complex with Mg(2+) and orthophosphate (1.8 A resolution), and in a complex with Mg(2+) and d-glycero-d-manno-heptose 1beta,7-bisphosphate (2.2 A resolution) were determined, in addition to the structure of Bordetella bronchiseptica GmhB bound to Mg(2+) and orthophosphate (1.7 A resolution). The structures show that in place of a cap domain, the GmhB catalytic site is elaborated by three peptide inserts or loops that pack to form a concave, semicircular surface around the substrate leaving group. Structure-guided kinetic analysis of site-directed mutants was conducted in parallel with a bioinformatics study of sequence diversification within the HisB subfamily to identify loop residues that serve as substrate recognition elements and that distinguish GmhB from its subfamily counterpart, the histidinol-phosphate phosphatase domain of HisB. We show that GmhB and the histidinol-phosphate phosphatase domain use the same design of three substrate recognition loops inserted into the cap domain yet, through selective residue usage on the loops, have achieved unique substrate specificity and thus novel biochemical function.

-	~~==Function==~~	+	Structural Determinants of Substrate Recognition in the HAD Superfamily Member d-glycero-d-manno-Heptose-1,7-bisphosphate Phosphatase (GmhB) .,Nguyen HH, Wang L, Huang H, Peisach E, Dunaway-Mariano D, Allen KN Biochemistry. 2010 Jan 22. PMID:20050614<ref>PMID:20050614</ref>
-	~~[[http://www.uniprot.org/uniprot/GMHB_ECOLI GMHB_ECOLI]] Converts~~ the D-glycero-~~beta-D~~-manno-~~heptose~~ 1,7-bisphosphate ~~intermediate into D-glycero-beta-D-manno-heptose 1-phosphate~~ (~~HBP~~) ~~by removing the phosphate group at the C-7 position~~. ~~Also catalyzes the dephosphorylation of fructose-1~~,6-~~bisphosphate (Fru1~~,~~6bisP)~~.~~<ref>~~PMID:~~11751812</ref>~~ <ref>PMID:~~16990279~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3l8e]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli Escherichia coli]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3L8E OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020050614</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Allen, K N.]]	+	[[Category: Allen, K N]]
-	[[Category: Nguyen, H.]]	+	[[Category: Nguyen, H]]
-	[[Category: Peisach, E.]]	+	[[Category: Peisach, E]]
	[[Category: 7-bisphosphate phosphatase]]		[[Category: 7-bisphosphate phosphatase]]
	[[Category: Carbohydrate metabolism]]		[[Category: Carbohydrate metabolism]]

OCA: Protected "3l8e" [edit=sysop:move=sysop]

OCA — Thu, 04 Apr 2013 20:14:38 GMT

Protected "3l8e" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:14, 4 April 2013

OCA at 20:14, 4 April 2013

OCA — Thu, 04 Apr 2013 20:14:34 GMT

←Older revision		Revision as of 20:14, 4 April 2013
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-	{{Seed}}
-	[[Image:3l8e.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3l8e", 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_3l8e\| PDB=3l8e \| SCENE= }}		{{STRUCTURE_3l8e\| PDB=3l8e \| SCENE= }}
-
	===Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli===		===Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli===
		+	{{ABSTRACT_PUBMED_20050614}}

-		+	==Function==
-	~~<!--~~	+	[[http://www.uniprot.org/uniprot/GMHB_ECOLI GMHB_ECOLI]] Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate (HBP) by removing the phosphate group at the C-7 position. Also catalyzes the dephosphorylation of fructose-1,6-bisphosphate (Fru1,6bisP).<ref>PMID:11751812</ref> <ref>PMID:16990279</ref>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_20050614}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov)~~, ~~where 20050614 is~~ the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_20050614}}~~	+

	==About this Structure==		==About this Structure==
-	~~3L8E~~ is a 2 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L8E OCA].	+	[[3l8e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L8E OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20050614~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020050614</ref><references group="xtra"/><references/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Allen, K N.]]		[[Category: Allen, K N.]]
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	[[Category: 7-bisphosphate phosphatase]]		[[Category: 7-bisphosphate phosphatase]]
	[[Category: Carbohydrate metabolism]]		[[Category: Carbohydrate metabolism]]
-	[[Category: Cytoplasm]]
	[[Category: D-glycero-d-manno-heptose-1]]		[[Category: D-glycero-d-manno-heptose-1]]
	[[Category: Gmhb]]		[[Category: Gmhb]]
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	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Lipopolysaccharide biosynthesis]]		[[Category: Lipopolysaccharide biosynthesis]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 25 09:33:25 2010''

OCA at 07:33, 25 February 2010

OCA — Thu, 25 Feb 2010 07:33:26 GMT

←Older revision		Revision as of 07:33, 25 February 2010
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	{{Seed}}		{{Seed}}
-	[[Image:3l8e.~~jpg~~\|left\|200px]]	+	[[Image:3l8e.png\|left\|200px]]

	<!--		<!--
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	[[Category: Lipopolysaccharide biosynthesis]]		[[Category: Lipopolysaccharide biosynthesis]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed~~ Feb 3 09:44:03 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 25 09:33:25 2010''

OCA at 07:44, 3 February 2010

OCA — Wed, 03 Feb 2010 07:44:04 GMT

←Older revision		Revision as of 07:44, 3 February 2010
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-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3l8e.jpg\|left\|200px]]

-	The ~~entry 3l8e~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3l8e", 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_3l8e\| PDB=3l8e \| SCENE= }}

-	~~Authors: Nguyen~~, H.~~, Peisach,~~ E.~~, Allen, K.N.~~	+	===Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli===

-	Description: Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jan 13 13~~:34:13 2010''	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20050614}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20050614 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20050614}}
		+
		+	==About this Structure==
		+	3L8E is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L8E OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20050614</ref><references group="xtra"/>
		+	[[Category: Escherichia coli]]
		+	[[Category: Allen, K N.]]
		+	[[Category: Nguyen, H.]]
		+	[[Category: Peisach, E.]]
		+	[[Category: 7-bisphosphate phosphatase]]
		+	[[Category: Carbohydrate metabolism]]
		+	[[Category: Cytoplasm]]
		+	[[Category: D-glycero-d-manno-heptose-1]]
		+	[[Category: Gmhb]]
		+	[[Category: Had superfamily]]
		+	[[Category: Hydrolase]]
		+	[[Category: Lipopolysaccharide biosynthesis]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 3 09:44:03 2010''

OCA at 11:34, 13 January 2010

OCA — Wed, 13 Jan 2010 11:34:13 GMT

←Older revision		Revision as of 11:34, 13 January 2010
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	The entry 3l8e is ON HOLD		The entry 3l8e is ON HOLD

-	Authors: Nguyen~~, H., Wang, L., Huang~~, H., Peisach, E~~., Dunaway-Mariano, D~~., Allen, K.N.	+	Authors: Nguyen, H., Peisach, E., Allen, K.N.

	Description: Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli		Description: Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan ~~6 09~~:14:51 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 13 13:34:13 2010''