2fpr - Revision history

OCA at 09:24, 14 February 2024

2024-02-14T09:24:51Z

← Older revision		Revision as of 09:24, 14 February 2024
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	<StructureSection load='2fpr' size='340' side='right'caption='[[2fpr]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2fpr' size='340' side='right'caption='[[2fpr]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fpr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Eco57 Eco57~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FPR FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fpr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FPR FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.7Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[2fps\|2fps]], [[2fpu\|2fpu]], [[2fpw\|2fpw]], [[2fpx\|2fpx]]~~</~~div~~><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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">hisB ([https~~:~~//www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td~~></tr>
	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Histidinol-phosphatase Histidinol-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.15 3.1.3.15]~~ </~~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=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [https://pdbe.org/2fpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB], [https://www.ebi.ac.uk/pdbsum/2fpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fpr 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=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [https://pdbe.org/2fpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB], [https://www.ebi.ac.uk/pdbsum/2fpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fpr ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[https://www.uniprot.org/uniprot/HIS7_ECO57 HIS7_ECO57]
	== 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=2fpr 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=2fpr ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	HisB from Escherichia coli is a bifunctional enzyme catalyzing the sixth and eighth steps of l-histidine biosynthesis. The N-terminal domain (HisB-N) possesses histidinol phosphate phosphatase activity, and its crystal structure shows a single domain with fold similarity to the haloacid dehalogenase (HAD) enzyme family. HisB-N forms dimers in the crystal and in solution. The structure shows the presence of a structural Zn(2+) ion stabilizing the conformation of an extended loop. Two metal binding sites were also identified in the active site. Their presence was further confirmed by isothermal titration calorimetry. HisB-N is active in the presence of Mg(2+), Mn(2+), Co(2+), or Zn(2+), but Ca(2+) has an inhibitory effect. We have determined structures of several intermediate states corresponding to snapshots along the reaction pathway, including that of the phosphoaspartate intermediate. A catalytic mechanism, different from that described for other HAD enzymes, is proposed requiring the presence of the second metal ion not found in the active sites of previously characterized HAD enzymes, to complete the second half-reaction. The proposed mechanism is reminiscent of two-Mg(2+) ion catalysis utilized by DNA and RNA polymerases and many nucleases. The structure also provides an explanation for the inhibitory effect of Ca(2+).

	Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway.,Rangarajan ES, Proteau A, Wagner J, Hung MN, Matte A, Cygler M J Biol Chem. 2006 Dec 8;281(49):37930-41. Epub 2006 Sep 11. PMID:16966333<ref>PMID:16966333</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2fpr" style="background-color:#fffaf0;"></div>~~
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Eco57]]~~		[[Category: Escherichia coli O157:H7]]
	~~[[Category~~: ~~Histidinol-phosphatase~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: Structural genomic]]~~		[[Category: Cygler M]]
	[[Category: Cygler, M]]		[[Category: Matte A]]
	[[Category: Matte, A]]		[[Category: Rangarajan ES]]
	[[Category: Rangarajan~~, E S]]~~
	~~[[Category: Bifunctional enzyme]]~~
	~~[[Category: Bsgi]]~~
	~~[[Category: Hisb]]~~
	~~[[Category: Histidinola phosphate phosphatase]]~~
	~~[[Category: Hydrolase~~]]

OCA at 15:31, 3 March 2021

2021-03-03T15:31:26Z

← Older revision		Revision as of 15:31, 3 March 2021
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	==Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model.==		==Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model.==
	<StructureSection load='2fpr' size='340' side='right' caption='[[2fpr]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2fpr' size='340' side='right'caption='[[2fpr]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fpr]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2FPR FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fpr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FPR FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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">[[2fps\|2fps]], [[2fpu\|2fpu]], [[2fpw\|2fpw]], [[2fpx\|2fpx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fps\|2fps]], [[2fpu\|2fpu]], [[2fpw\|2fpw]], [[2fpx\|2fpx]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hisB ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hisB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Histidinol-phosphatase Histidinol-phosphatase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.15 3.1.3.15] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histidinol-phosphatase Histidinol-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.15 3.1.3.15] </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=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [~~http~~://pdbe.org/2fpr PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2fpr PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2fpr 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=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [https://pdbe.org/2fpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB], [https://www.ebi.ac.uk/pdbsum/2fpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fpr ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	[[Category: Eco57]]		[[Category: Eco57]]
	[[Category: Histidinol-phosphatase]]		[[Category: Histidinol-phosphatase]]
			[[Category: Large Structures]]
	[[Category: Structural genomic]]		[[Category: Structural genomic]]
	[[Category: Cygler, M]]		[[Category: Cygler, M]]

OCA at 18:49, 24 January 2018

2018-01-24T18:49:33Z

← Older revision		Revision as of 18:49, 24 January 2018
Line 1:		Line 1:

	==Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model.==		==Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model.==
	<StructureSection load='2fpr' size='340' side='right' caption='[[2fpr]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2fpr' size='340' side='right' caption='[[2fpr]], [[Resolution\|resolution]] 1.70Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hisB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hisB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphatase Histidinol-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.15 3.1.3.15] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphatase Histidinol-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.15 3.1.3.15] </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=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [http://pdbe.org/2fpr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB], [http://www.ebi.ac.uk/pdbsum/2fpr 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=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [http://pdbe.org/2fpr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB], [http://www.ebi.ac.uk/pdbsum/2fpr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fpr ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/2fpr_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/2fpr_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 17:34, 8 February 2016

2016-02-08T17:34:43Z

← Older revision		Revision as of 17:34, 8 February 2016
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	<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=2fpr ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 13:52, 10 September 2015

2015-09-10T13:52:11Z

← Older revision		Revision as of 13:52, 10 September 2015
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	<StructureSection load='2fpr' size='340' side='right' caption='[[2fpr]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2fpr' size='340' side='right' caption='[[2fpr]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fpr]] 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=2FPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FPR FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fpr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FPR FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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">[[2fps\|2fps]], [[2fpu\|2fpu]], [[2fpw\|2fpw]], [[2fpx\|2fpx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fps\|2fps]], [[2fpu\|2fpu]], [[2fpw\|2fpw]], [[2fpx\|2fpx]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hisB ([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">hisB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphatase Histidinol-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.15 3.1.3.15] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphatase Histidinol-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.15 3.1.3.15] </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=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB], [http://www.ebi.ac.uk/pdbsum/2fpr 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=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [http://pdbe.org/2fpr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB], [http://www.ebi.ac.uk/pdbsum/2fpr PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	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 2fpr" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Escherichia coli~~]]		[[Category: Eco57]]
	[[Category: Histidinol-phosphatase]]		[[Category: Histidinol-phosphatase]]
	[[Category: Structural genomic]]		[[Category: Structural genomic]]

OCA at 08:40, 16 January 2015

2015-01-16T08:40:52Z

← Older revision		Revision as of 08:40, 16 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fpr]] 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=2FPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FPR FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fpr]] 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=2FPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FPR FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fps\|2fps]], [[2fpu\|2fpu]], [[2fpw\|2fpw]], [[2fpx\|2fpx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fps\|2fps]], [[2fpu\|2fpu]], [[2fpw\|2fpw]], [[2fpx\|2fpx]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hisB ([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">hisB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphatase Histidinol-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.15 3.1.3.15] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphatase Histidinol-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.15 3.1.3.15] </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=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB], [http://www.ebi.ac.uk/pdbsum/2fpr 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=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB], [http://www.ebi.ac.uk/pdbsum/2fpr 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:
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Histidinol-phosphatase]]		[[Category: Histidinol-phosphatase]]
	[[Category: ~~BSGI, Montreal-Kingston Bacterial~~ Structural ~~Genomics Initiative.~~]]		[[Category: Structural genomic]]
	[[Category: Cygler, M]]		[[Category: Cygler, M]]
	[[Category: Matte, A.]]		[[Category: Matte, A]]
	[[Category: Rangarajan, E S~~.]]~~		[[Category: Rangarajan, E S]]
	~~[[Category: Bacterial structure genomic~~]]		[[Category: Bifunctional enzyme]]
	[[Category: Bifunctional enzyme.]]
	[[Category: Bsgi]]		[[Category: Bsgi]]
	[[Category: Hisb]]		[[Category: Hisb]]
	[[Category: Histidinola phosphate phosphatase]]		[[Category: Histidinola phosphate phosphatase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	~~[[Category: Montreal-kingston bacterial structural genomics initiative]]~~
	~~[[Category: Structural genomic]]~~

OCA at 08:19, 30 September 2014

2014-09-30T08:19:08Z

← Older revision		Revision as of 08:19, 30 September 2014
Line 1:		Line 1:
	[[Image:~~2fpr~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model.==
			<StructureSection load='2fpr' size='340' side='right' caption='[[2fpr]], [[Resolution\|resolution]] 1.70Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2fpr]] 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=2FPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FPR FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fps\|2fps]], [[2fpu\|2fpu]], [[2fpw\|2fpw]], [[2fpx\|2fpx]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hisB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphatase Histidinol-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.15 3.1.3.15] </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=2fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fpr RCSB], [http://www.ebi.ac.uk/pdbsum/2fpr 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/fp/2fpr_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 ==
			HisB from Escherichia coli is a bifunctional enzyme catalyzing the sixth and eighth steps of l-histidine biosynthesis. The N-terminal domain (HisB-N) possesses histidinol phosphate phosphatase activity, and its crystal structure shows a single domain with fold similarity to the haloacid dehalogenase (HAD) enzyme family. HisB-N forms dimers in the crystal and in solution. The structure shows the presence of a structural Zn(2+) ion stabilizing the conformation of an extended loop. Two metal binding sites were also identified in the active site. Their presence was further confirmed by isothermal titration calorimetry. HisB-N is active in the presence of Mg(2+), Mn(2+), Co(2+), or Zn(2+), but Ca(2+) has an inhibitory effect. We have determined structures of several intermediate states corresponding to snapshots along the reaction pathway, including that of the phosphoaspartate intermediate. A catalytic mechanism, different from that described for other HAD enzymes, is proposed requiring the presence of the second metal ion not found in the active sites of previously characterized HAD enzymes, to complete the second half-reaction. The proposed mechanism is reminiscent of two-Mg(2+) ion catalysis utilized by DNA and RNA polymerases and many nucleases. The structure also provides an explanation for the inhibitory effect of Ca(2+).

	~~{{STRUCTURE_2fpr\| PDB=2fpr \| SCENE= }}~~		Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway.,Rangarajan ES, Proteau A, Wagner J, Hung MN, Matte A, Cygler M J Biol Chem. 2006 Dec 8;281(49):37930-41. Epub 2006 Sep 11. PMID:16966333<ref>PMID:16966333</ref>

	~~===Crystal structure~~ the ~~N-terminal domain of E~~. ~~coli HisB~~. ~~Apo Mg model~~.~~===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_16966333}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[2fpr]] 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=2FPR OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:016966333<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Histidinol-phosphatase]]		[[Category: Histidinol-phosphatase]]

OCA: Protected "2fpr" [edit=sysop:move=sysop]

2013-01-07T13:21:51Z

Protected "2fpr" [edit=sysop:move=sysop]

← Older revision	Revision as of 13:21, 7 January 2013
(No difference)

OCA at 13:21, 7 January 2013

2013-01-07T13:21:48Z

← Older revision		Revision as of 13:21, 7 January 2013
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	~~{{Seed}}~~
	[[Image:2fpr.png\|left\|200px]]		[[Image:2fpr.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2fpr", 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_2fpr\| PDB=2fpr \| SCENE= }}		{{STRUCTURE_2fpr\| PDB=2fpr \| SCENE= }}

	===Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model.===		===Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model.===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_16966333}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 16966333 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_16966333}}		{{ABSTRACT_PUBMED_16966333}}

	==About this Structure==		==About this Structure==
	~~2FPR~~ is a 2 ~~chains~~ structure ~~of 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=2FPR OCA].		[[2fpr]] 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=2FPR OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~16966333~~</ref><references group="xtra"/>		<ref group="xtra">PMID:016966333</ref><references group="xtra"/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Histidinol-phosphatase]]		[[Category: Histidinol-phosphatase]]
Line 35:		Line 23:
	[[Category: Hisb]]		[[Category: Hisb]]
	[[Category: Histidinola phosphate phosphatase]]		[[Category: Histidinola phosphate phosphatase]]
			[[Category: Hydrolase]]
	[[Category: Montreal-kingston bacterial structural genomics initiative]]		[[Category: Montreal-kingston bacterial structural genomics initiative]]
	[[Category: Structural genomic]]		[[Category: Structural genomic]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 00:49:35 2009''~~

OCA at 22:49, 16 February 2009

2009-02-16T22:49:37Z

← Older revision		Revision as of 22:49, 16 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
	2FPR is a ~~[[Single protein]]~~ structure of ~~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=2FPR OCA].		2FPR is a 2 chains structure of 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=2FPR OCA].

	==Reference==		==Reference==
	Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway., Rangarajan ES, Proteau A, Wagner J, Hung MN, Matte A, Cygler M, J Biol Chem. 2006 Dec 8;281(49):37930-41. Epub 2006 Sep 11. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/16966333 16966333]~~		<ref group="xtra">PMID:16966333</ref><references group="xtra"/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Histidinol-phosphatase]]		[[Category: Histidinol-phosphatase]]
	~~[[Category: Single protein]]~~
	[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]		[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
	[[Category: Cygler, M]]		[[Category: Cygler, M]]
Line 39:		Line 38:
	[[Category: Structural genomic]]		[[Category: Structural genomic]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Jul 28 05~~:19:~~58 2008~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 00:49:35 2009''