1l8o - Revision history

OCA at 08:07, 3 April 2024

OCA — Wed, 03 Apr 2024 08:07:32 GMT

←Older revision		Revision as of 08:07, 3 April 2024
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	<StructureSection load='1l8o' size='340' side='right'caption='[[1l8o]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1l8o' size='340' side='right'caption='[[1l8o]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1l8o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L8O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1l8o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L8O FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>~~, ~~<scene name='pdbligand=SER:SERINE'>SER</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;~~'>~~[[1l8l\|1l8l]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3]~~ </~~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=1l8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8o OCA], [https://pdbe.org/1l8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l8o RCSB], [https://www.ebi.ac.uk/pdbsum/1l8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l8o 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=1l8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8o OCA], [https://pdbe.org/1l8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l8o RCSB], [https://www.ebi.ac.uk/pdbsum/1l8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l8o ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:[https://omim.org/entry/614023 614023]]. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.<ref>PMID:14673469</ref>	+	[https://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN] Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:[https://omim.org/entry/614023 614023]. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.<ref>PMID:14673469</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates.<ref>PMID:12777757</ref>	+	[https://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN] Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates.<ref>PMID:12777757</ref>
	== 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=1l8o 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=1l8o ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Human phosphoserine phosphatase (HPSP) regulates the levels of glycine and d-serine, the putative co-agonists for the glycine site of the NMDA receptor in the brain. Here, we describe the first crystal structures of the HPSP in complexes with the competitive inhibitor 2-amino-3-phosphonopropionic acid (AP3) at 2.5 A, and the phosphate ion (Pi) and the product uncompetitive inhibitor l-serine (HPSP.l-Ser.Pi) at 2.8 A. The complex structures reveal that the open-closed environmental change of the active site, generated by local rearrangement of the alpha-helical bundle domain, is important to substrate recognition and hydrolysis. The maximal extent of this structural rearrangement is shown to be about 13 A at the L4 loop and about 25 degrees at the helix alpha3. Both the structural change and mutagenesis data suggest that Arg-65 and Glu-29 play an important role in the binding of the substrate. Interestingly, the AP3 binding mode turns out to be significantly different from that of the natural substrate, phospho-l-serine, and the HPSP.l-Ser.Pi structure provides a structural basis for the feedback control mechanism of serine. These analyses allow us to provide a clear model for the mechanism of HPSP and a framework for structure-based drug development.
-
-	Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase.,Kim HY, Heo YS, Kim JH, Park MH, Moon J, Kim E, Kwon D, Yoon J, Shin D, Jeong EJ, Park SY, Lee TG, Jeon YH, Ro S, Cho JM, Hwang KY J Biol Chem. 2002 Nov 29;277(48):46651-8. Epub 2002 Sep 3. PMID:12213811<ref>PMID:12213811</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1l8o" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Phosphoserine phosphatase]]~~	+	[[Category: Heo YS]]
-	[[Category: Heo~~, Y S~~]]	+	[[Category: Hwang KY]]
-	[[Category: Hwang~~, K Y~~]]	+	[[Category: Jeon YH]]
-	[[Category: Jeon~~, Y H~~]]	+	[[Category: Kim HY]]
-	[[Category: Kim~~, H Y~~]]	+	[[Category: Kim JH]]
-	[[Category: Kim~~, J H~~]]	+	[[Category: Lee TG]]
-	[[Category: Lee~~, T G~~]]	+	[[Category: Moon J]]
-	[[Category: Moon, J]]	+	[[Category: Park MH]]
-	[[Category: Park~~, M H~~]]	+	[[Category: Park SY]]
-	[[Category: Park~~, S Y~~]]	+	[[Category: Ro S]]
-	[[Category: Ro, S]]	+
-	~~[[Category: Conformational rearrangement]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Phosphatase~~]]	+

OCA at 06:41, 18 August 2021

OCA — Wed, 18 Aug 2021 06:41:25 GMT

OCA at 12:08, 13 November 2019

OCA — Wed, 13 Nov 2019 12:08:28 GMT

←Older revision		Revision as of 12:08, 13 November 2019
Line 1:		Line 1:

	==Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase==		==Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase==
-	<StructureSection load='1l8o' size='340' side='right' caption='[[1l8o]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='1l8o' size='340' side='right'caption='[[1l8o]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1l8o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L8O FirstGlance]. <br>		<table><tr><td colspan='2'>[[1l8o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L8O FirstGlance]. <br>
Line 32:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 1l8o" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1l8o" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Phosphoserine phosphatase\|Phosphoserine phosphatase]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Phosphoserine phosphatase]]		[[Category: Phosphoserine phosphatase]]
	[[Category: Heo, Y S]]		[[Category: Heo, Y S]]

OCA at 21:18, 24 January 2018

OCA — Wed, 24 Jan 2018 21:18:30 GMT

←Older revision		Revision as of 21:18, 24 January 2018
Line 1:		Line 1:
		+
	==Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase==		==Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase==
	<StructureSection load='1l8o' size='340' side='right' caption='[[1l8o]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1l8o' size='340' side='right' caption='[[1l8o]], [[Resolution\|resolution]] 2.80Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l8l\|1l8l]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l8l\|1l8l]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </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=1l8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8o OCA], [http://pdbe.org/1l8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l8o RCSB], [http://www.ebi.ac.uk/pdbsum/1l8o 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=1l8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8o OCA], [http://pdbe.org/1l8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l8o RCSB], [http://www.ebi.ac.uk/pdbsum/1l8o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l8o ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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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/l8/1l8o_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l8/1l8o_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 31:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 1l8o" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1l8o" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Phosphoserine phosphatase\|Phosphoserine phosphatase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:21, 7 February 2016

OCA — Sun, 07 Feb 2016 20:21:00 GMT

←Older revision		Revision as of 20:21, 7 February 2016
Line 20:		Line 20:
	<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=1l8o ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 04:41, 10 September 2015

OCA — Thu, 10 Sep 2015 04:41:30 GMT

←Older revision		Revision as of 04:41, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1l8o' size='340' side='right' caption='[[1l8o]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1l8o' size='340' side='right' caption='[[1l8o]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1l8o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L8O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1l8o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L8O FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l8l\|1l8l]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l8l\|1l8l]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </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=1l8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l8o RCSB], [http://www.ebi.ac.uk/pdbsum/1l8o 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=1l8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8o OCA], [http://pdbe.org/1l8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l8o RCSB], [http://www.ebi.ac.uk/pdbsum/1l8o PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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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 1l8o" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Phosphoserine phosphatase]]		[[Category: Phosphoserine phosphatase]]
	[[Category: Heo, Y S]]		[[Category: Heo, Y S]]

OCA at 16:27, 5 January 2015

OCA — Mon, 05 Jan 2015 16:27:30 GMT

←Older revision		Revision as of 16:27, 5 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1l8o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L8O FirstGlance]. <br>		<table><tr><td colspan='2'>[[1l8o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L8O FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l8l\|1l8l]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l8l\|1l8l]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </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=1l8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l8o RCSB], [http://www.ebi.ac.uk/pdbsum/1l8o 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=1l8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l8o RCSB], [http://www.ebi.ac.uk/pdbsum/1l8o PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:[http://omim.org/entry/614023 614023]]. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.<ref>PMID:14673469</ref>		[[http://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:[http://omim.org/entry/614023 614023]]. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.<ref>PMID:14673469</ref>
Line 39:		Line 39:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoserine phosphatase]]		[[Category: Phosphoserine phosphatase]]
-	[[Category: Heo, Y S.]]	+	[[Category: Heo, Y S]]
-	[[Category: Hwang, K Y.]]	+	[[Category: Hwang, K Y]]
-	[[Category: Jeon, Y H.]]	+	[[Category: Jeon, Y H]]
-	[[Category: Kim, H Y.]]	+	[[Category: Kim, H Y]]
-	[[Category: Kim, J H.]]	+	[[Category: Kim, J H]]
-	[[Category: Lee, T G.]]	+	[[Category: Lee, T G]]
-	[[Category: Moon, J.]]	+	[[Category: Moon, J]]
-	[[Category: Park, M H.]]	+	[[Category: Park, M H]]
-	[[Category: Park, S Y.]]	+	[[Category: Park, S Y]]
-	[[Category: Ro, S.]]	+	[[Category: Ro, S]]
	[[Category: Conformational rearrangement]]		[[Category: Conformational rearrangement]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Phosphatase]]		[[Category: Phosphatase]]

OCA at 14:27, 29 September 2014

OCA — Mon, 29 Sep 2014 14:27:57 GMT

←Older revision		Revision as of 14:27, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1l8o\| PDB=1l8o \| SCENE= }}~~	+	==Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase==
-	===Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase===	+	<StructureSection load='1l8o' size='340' side='right' caption='[[1l8o]], [[Resolution\|resolution]] 2.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_12213811}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1l8o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L8O FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l8l\|1l8l]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </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=1l8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l8o RCSB], [http://www.ebi.ac.uk/pdbsum/1l8o PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:[http://omim.org/entry/614023 614023]]. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.<ref>PMID:14673469</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates.<ref>PMID:12777757</ref>
		+	== 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/l8/1l8o_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 ==
		+	Human phosphoserine phosphatase (HPSP) regulates the levels of glycine and d-serine, the putative co-agonists for the glycine site of the NMDA receptor in the brain. Here, we describe the first crystal structures of the HPSP in complexes with the competitive inhibitor 2-amino-3-phosphonopropionic acid (AP3) at 2.5 A, and the phosphate ion (Pi) and the product uncompetitive inhibitor l-serine (HPSP.l-Ser.Pi) at 2.8 A. The complex structures reveal that the open-closed environmental change of the active site, generated by local rearrangement of the alpha-helical bundle domain, is important to substrate recognition and hydrolysis. The maximal extent of this structural rearrangement is shown to be about 13 A at the L4 loop and about 25 degrees at the helix alpha3. Both the structural change and mutagenesis data suggest that Arg-65 and Glu-29 play an important role in the binding of the substrate. Interestingly, the AP3 binding mode turns out to be significantly different from that of the natural substrate, phospho-l-serine, and the HPSP.l-Ser.Pi structure provides a structural basis for the feedback control mechanism of serine. These analyses allow us to provide a clear model for the mechanism of HPSP and a framework for structure-based drug development.

-	~~==Disease==~~	+	Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase.,Kim HY, Heo YS, Kim JH, Park MH, Moon J, Kim E, Kwon D, Yoon J, Shin D, Jeong EJ, Park SY, Lee TG, Jeon YH, Ro S, Cho JM, Hwang KY J Biol Chem. 2002 Nov 29;277(48):46651-8. Epub 2002 Sep 3. PMID:12213811<ref>PMID:12213811</ref>
-	~~[[http://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Defects in PSPH are~~ the ~~cause~~ of phosphoserine phosphatase ~~deficiency~~ (~~PSPHD~~)~~[MIM~~:~~[http://omim.org/entry/614023 614023]]. A disorder that results in pre~~- ~~and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome~~.<ref>PMID:~~14673469~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www~~.~~uniprot~~.~~org/uniprot/SERB_HUMAN SERB_HUMAN]] Catalyzes the last step in the biosynthesis~~ of ~~serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates~~.<~~ref~~>~~PMID:12777757~~</~~ref~~>	+	</div>
-		+
-	~~==About this Structure==~~	+
-	[[1l8o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA].	+

	==See Also==		==See Also==
	*[[Phosphoserine phosphatase\|Phosphoserine phosphatase]]		*[[Phosphoserine phosphatase\|Phosphoserine phosphatase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:012213811</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoserine phosphatase]]		[[Category: Phosphoserine phosphatase]]

OCA at 23:59, 24 March 2013

OCA — Sun, 24 Mar 2013 23:59:45 GMT

←Older revision		Revision as of 23:59, 24 March 2013
Line 1:		Line 1:
-	[[Image:1l8o.png\|left\|200px]]
-
	{{STRUCTURE_1l8o\| PDB=1l8o \| SCENE= }}		{{STRUCTURE_1l8o\| PDB=1l8o \| SCENE= }}
-
	===Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase===		===Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase===
		+	{{ABSTRACT_PUBMED_12213811}}

-	~~{{ABSTRACT_PUBMED_12213811}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:[http://omim.org/entry/614023 614023]]. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.<ref>PMID:14673469</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates.<ref>PMID:12777757</ref>

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:012213811</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012213811</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoserine phosphatase]]		[[Category: Phosphoserine phosphatase]]

OCA at 07:46, 20 October 2012

OCA — Sat, 20 Oct 2012 07:46:05 GMT

←Older revision		Revision as of 07:46, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1l8o]] is a 2 chain structure ~~of [[Phosphoserine phosphatase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA].	+	[[1l8o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA].

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

←Older revision		Revision as of 06:41, 18 August 2021
Line 3:		Line 3:
	<StructureSection load='1l8o' size='340' side='right'caption='[[1l8o]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1l8o' size='340' side='right'caption='[[1l8o]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1l8o]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1L8O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1l8o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L8O FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l8l\|1l8l]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l8l\|1l8l]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </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=1l8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8o OCA], [~~http~~://pdbe.org/1l8o PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1l8o RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1l8o PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1l8o 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=1l8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8o OCA], [https://pdbe.org/1l8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l8o RCSB], [https://www.ebi.ac.uk/pdbsum/1l8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l8o ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:[~~http~~://omim.org/entry/614023 614023]]. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.<ref>PMID:14673469</ref>	+	[[https://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:[https://omim.org/entry/614023 614023]]. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.<ref>PMID:14673469</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates.<ref>PMID:12777757</ref>	+	[[https://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates.<ref>PMID:12777757</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]