1qwo - Revision history

OCA at 06:07, 17 April 2024

OCA — Wed, 17 Apr 2024 06:07:50 GMT

←Older revision		Revision as of 06:07, 17 April 2024
Line 3:		Line 3:
	<StructureSection load='1qwo' size='340' side='right'caption='[[1qwo]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='1qwo' size='340' side='right'caption='[[1qwo]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qwo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QWO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qwo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QWO FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=NAG:N~~-~~ACETYL-D-GLUCOSAMINE'>NAG</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]] 1.5Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~NEP~~:N1-~~PHOSPHONOHISTIDINE~~'>~~NEP~~</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8]~~ </~~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=1qwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwo OCA], [https://pdbe.org/1qwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qwo RCSB], [https://www.ebi.ac.uk/pdbsum/1qwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwo 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=1qwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwo OCA], [https://pdbe.org/1qwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qwo RCSB], [https://www.ebi.ac.uk/pdbsum/1qwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PHYA_ASPFU PHYA_ASPFU]] Catalyzes the hydrolysis of inorganic orthophosphate from phytate.	+	[https://www.uniprot.org/uniprot/PHYA_ASPFU PHYA_ASPFU] Catalyzes the hydrolysis of inorganic orthophosphate from phytate.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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=1qwo 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=1qwo ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	In order to understand the structural basis for the high thermostability of phytase from Aspergillus fumigatus, its crystal structure was determined at 1.5 A resolution. The overall fold resembles the structure of other phytase enzymes. Aspergillus niger phytase shares 66% sequence identity, however, it is much less heat-resistant. A superimposition of these two structures reveals some significant differences. In particular, substitutions with polar residues appear to remove repulsive ion pair interactions and instead form hydrogen bond interactions, which stabilize the enzyme; the formation of a C-terminal helical capping, induced by arginine residue substitutions also appears to be critical for the enzyme's ability to refold to its active form after denaturation at high temperature. The heat-resilient property of A.fumigatus phytase could be due to the improved stability of regions that are critical for the refolding of the protein; and a heat-resistant A.niger phytase may be achieved by mutating certain critical residues with the equivalent residues in A.fumigatus phytase. Six predicted N-glycosylation sites were observed to be glycosylated from the experimental electron density. Furthermore, the enzyme's catalytic residue His59 was found to be partly phosphorylated and thus showed a reaction intermediate, providing structural insight, which may help understand the catalytic mechanism of the acid phosphatase family. The trap of this catalytic intermediate confirms the two-step catalytic mechanism of the acid histidine phosphatase family.

-	Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine.,Xiang T, Liu Q, Deacon AM, Koshy M, Kriksunov IA, Lei XG, Hao Q, Thiel DJ J Mol Biol. 2004 May 28;339(2):437-45. PMID:15136045<ref>PMID:15136045</ref>	+	==See Also==
-		+	*[[Phytase 3D structures\|Phytase 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 1qwo" style="background-color:#fffaf0;"></div>~~	+
-	== ~~References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~3-phytase~~]]	+	[[Category: Aspergillus fumigatus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Deacon~~, A M~~]]	+	[[Category: Deacon AM]]
-	[[Category: Hao, Q]]	+	[[Category: Hao Q]]
-	[[Category: Koshy, M]]	+	[[Category: Koshy M]]
-	[[Category: Kriksunov~~, I A~~]]	+	[[Category: Kriksunov IA]]
-	[[Category: Lei~~, X G~~]]	+	[[Category: Lei XG]]
-	[[Category: Liu, Q]]	+	[[Category: Liu Q]]
-	[[Category: Thiel~~, D J~~]]	+	[[Category: Thiel DJ]]
-	[[Category: Xiang, T]]	+	[[Category: Xiang T]]
-	~~[[Category: Alpha barrel]]~~	+
-	~~[[Category: Beta sandwich]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Orthogonal bundle]]~~	+
-	~~[[Category: Phosphohistidine~~]]	+

OCA at 10:05, 15 September 2021

OCA — Wed, 15 Sep 2021 10:05:36 GMT

←Older revision		Revision as of 10:05, 15 September 2021
Line 3:		Line 3:
	<StructureSection load='1qwo' size='340' side='right'caption='[[1qwo]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='1qwo' size='340' side='right'caption='[[1qwo]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qwo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1QWO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qwo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QWO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </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=1qwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwo OCA], [~~http~~://pdbe.org/1qwo PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1qwo RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1qwo PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwo 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=1qwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwo OCA], [https://pdbe.org/1qwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qwo RCSB], [https://www.ebi.ac.uk/pdbsum/1qwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PHYA_ASPFU PHYA_ASPFU]] Catalyzes the hydrolysis of inorganic orthophosphate from phytate.	+	[[https://www.uniprot.org/uniprot/PHYA_ASPFU PHYA_ASPFU]] Catalyzes the hydrolysis of inorganic orthophosphate from phytate.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 11:32, 4 December 2019

OCA — Wed, 04 Dec 2019 11:32:21 GMT

←Older revision		Revision as of 11:32, 4 December 2019
Line 1:		Line 1:

	==Crystal structure of a phosphorylated phytase from Aspergillus fumigatus, revealing the structural basis for its heat resilience and catalytic pathway==		==Crystal structure of a phosphorylated phytase from Aspergillus fumigatus, revealing the structural basis for its heat resilience and catalytic pathway==
-	<StructureSection load='1qwo' size='340' side='right' caption='[[1qwo]], [[Resolution\|resolution]] 1.50Å' scene=''>	+	<StructureSection load='1qwo' size='340' side='right'caption='[[1qwo]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1qwo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QWO FirstGlance]. <br>		<table><tr><td colspan='2'>[[1qwo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QWO FirstGlance]. <br>
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: 3-phytase]]		[[Category: 3-phytase]]
		+	[[Category: Large Structures]]
	[[Category: Deacon, A M]]		[[Category: Deacon, A M]]
	[[Category: Hao, Q]]		[[Category: Hao, Q]]

OCA at 07:57, 28 February 2018

OCA — Wed, 28 Feb 2018 07:57:22 GMT

←Older revision		Revision as of 07:57, 28 February 2018
Line 1:		Line 1:
		+
	==Crystal structure of a phosphorylated phytase from Aspergillus fumigatus, revealing the structural basis for its heat resilience and catalytic pathway==		==Crystal structure of a phosphorylated phytase from Aspergillus fumigatus, revealing the structural basis for its heat resilience and catalytic pathway==
	<StructureSection load='1qwo' size='340' side='right' caption='[[1qwo]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='1qwo' size='340' side='right' caption='[[1qwo]], [[Resolution\|resolution]] 1.50Å' scene=''>
Line 6:		Line 7:
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </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=1qwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwo OCA], [http://pdbe.org/1qwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qwo RCSB], [http://www.ebi.ac.uk/pdbsum/1qwo 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=1qwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwo OCA], [http://pdbe.org/1qwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qwo RCSB], [http://www.ebi.ac.uk/pdbsum/1qwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qw/1qwo_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qw/1qwo_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 17:05, 7 February 2016

OCA — Sun, 07 Feb 2016 17:05:25 GMT

←Older revision		Revision as of 17:05, 7 February 2016
Line 18:		Line 18:
	<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=1qwo ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 03:29, 10 September 2015

OCA — Thu, 10 Sep 2015 03:29:11 GMT

←Older revision		Revision as of 03:29, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1qwo' size='340' side='right' caption='[[1qwo]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='1qwo' size='340' side='right' caption='[[1qwo]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qwo]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QWO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qwo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QWO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </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=1qwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qwo RCSB], [http://www.ebi.ac.uk/pdbsum/1qwo 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=1qwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwo OCA], [http://pdbe.org/1qwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qwo RCSB], [http://www.ebi.ac.uk/pdbsum/1qwo PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 1qwo" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: 3-phytase]]		[[Category: 3-phytase]]
-	[[Category: Aspergillus fumigatus]]
	[[Category: Deacon, A M]]		[[Category: Deacon, A M]]
	[[Category: Hao, Q]]		[[Category: Hao, Q]]

OCA at 16:54, 24 December 2014

OCA — Wed, 24 Dec 2014 16:54:24 GMT

←Older revision		Revision as of 16:54, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1qwo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QWO FirstGlance]. <br>		<table><tr><td colspan='2'>[[1qwo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QWO FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </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=1qwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qwo RCSB], [http://www.ebi.ac.uk/pdbsum/1qwo 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=1qwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qwo RCSB], [http://www.ebi.ac.uk/pdbsum/1qwo PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PHYA_ASPFU PHYA_ASPFU]] Catalyzes the hydrolysis of inorganic orthophosphate from phytate.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: 3-phytase]]		[[Category: 3-phytase]]
	[[Category: Aspergillus fumigatus]]		[[Category: Aspergillus fumigatus]]
-	[[Category: Deacon, A M.]]	+	[[Category: Deacon, A M]]
-	[[Category: Hao, Q.]]	+	[[Category: Hao, Q]]
-	[[Category: Koshy, M.]]	+	[[Category: Koshy, M]]
-	[[Category: Kriksunov, I A.]]	+	[[Category: Kriksunov, I A]]
-	[[Category: Lei, X G.]]	+	[[Category: Lei, X G]]
-	[[Category: Liu, Q.]]	+	[[Category: Liu, Q]]
-	[[Category: Thiel, D J.]]	+	[[Category: Thiel, D J]]
-	[[Category: Xiang, T.]]	+	[[Category: Xiang, T]]
	[[Category: Alpha barrel]]		[[Category: Alpha barrel]]
	[[Category: Beta sandwich]]		[[Category: Beta sandwich]]

OCA at 17:29, 29 September 2014

OCA — Mon, 29 Sep 2014 17:29:00 GMT

←Older revision		Revision as of 17:29, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1qwo.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of a phosphorylated phytase from Aspergillus fumigatus, revealing the structural basis for its heat resilience and catalytic pathway==
		+	<StructureSection load='1qwo' size='340' side='right' caption='[[1qwo]], [[Resolution\|resolution]] 1.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1qwo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QWO FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </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=1qwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qwo RCSB], [http://www.ebi.ac.uk/pdbsum/1qwo 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/qw/1qwo_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 ==
		+	In order to understand the structural basis for the high thermostability of phytase from Aspergillus fumigatus, its crystal structure was determined at 1.5 A resolution. The overall fold resembles the structure of other phytase enzymes. Aspergillus niger phytase shares 66% sequence identity, however, it is much less heat-resistant. A superimposition of these two structures reveals some significant differences. In particular, substitutions with polar residues appear to remove repulsive ion pair interactions and instead form hydrogen bond interactions, which stabilize the enzyme; the formation of a C-terminal helical capping, induced by arginine residue substitutions also appears to be critical for the enzyme's ability to refold to its active form after denaturation at high temperature. The heat-resilient property of A.fumigatus phytase could be due to the improved stability of regions that are critical for the refolding of the protein; and a heat-resistant A.niger phytase may be achieved by mutating certain critical residues with the equivalent residues in A.fumigatus phytase. Six predicted N-glycosylation sites were observed to be glycosylated from the experimental electron density. Furthermore, the enzyme's catalytic residue His59 was found to be partly phosphorylated and thus showed a reaction intermediate, providing structural insight, which may help understand the catalytic mechanism of the acid phosphatase family. The trap of this catalytic intermediate confirms the two-step catalytic mechanism of the acid histidine phosphatase family.

-	~~{{STRUCTURE_1qwo\| PDB=1qwo \| SCENE= }}~~	+	Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine.,Xiang T, Liu Q, Deacon AM, Koshy M, Kriksunov IA, Lei XG, Hao Q, Thiel DJ J Mol Biol. 2004 May 28;339(2):437-45. PMID:15136045<ref>PMID:15136045</ref>

-	~~===Crystal structure~~ of ~~a phosphorylated phytase from Aspergillus fumigatus, revealing~~ the ~~structural basis for its heat resilience and catalytic pathway===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15136045}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1qwo]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:015136045<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: 3-phytase]]		[[Category: 3-phytase]]
	[[Category: Aspergillus fumigatus]]		[[Category: Aspergillus fumigatus]]

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

OCA — Wed, 02 Jan 2013 09:47:01 GMT

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

←Older revision

Revision as of 09:47, 2 January 2013

OCA at 09:46, 2 January 2013

OCA — Wed, 02 Jan 2013 09:46:59 GMT

←Older revision		Revision as of 09:46, 2 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1qwo.png\|left\|200px]]		[[Image:1qwo.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1qwo", 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_1qwo\| PDB=1qwo \| SCENE= }}		{{STRUCTURE_1qwo\| PDB=1qwo \| SCENE= }}

	===Crystal structure of a phosphorylated phytase from Aspergillus fumigatus, revealing the structural basis for its heat resilience and catalytic pathway===		===Crystal structure of a phosphorylated phytase from Aspergillus fumigatus, revealing the structural basis for its heat resilience and catalytic pathway===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15136045}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15136045 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_15136045}}		{{ABSTRACT_PUBMED_15136045}}

	==About this Structure==		==About this Structure==
-	~~1QWO~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA].	+	[[1qwo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWO OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15136045~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015136045</ref><references group="xtra"/>
	[[Category: 3-phytase]]		[[Category: 3-phytase]]
	[[Category: Aspergillus fumigatus]]		[[Category: Aspergillus fumigatus]]
Line 40:		Line 28:
	[[Category: Orthogonal bundle]]		[[Category: Orthogonal bundle]]
	[[Category: Phosphohistidine]]		[[Category: Phosphohistidine]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 18:13:58 2009''