1ore - Revision history

OCA at 08:02, 14 February 2024

OCA — Wed, 14 Feb 2024 08:02:32 GMT

←Older revision		Revision as of 08:02, 14 February 2024
Line 3:		Line 3:
	<StructureSection load='1ore' size='340' side='right'caption='[[1ore]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1ore' size='340' side='right'caption='[[1ore]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ore]] is a 1 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=1ORE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1ORE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ore]] is a 1 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=1ORE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ORE FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>~~, ~~<scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.1Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>APRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase Adenine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.7 2.4.2.7]~~ </~~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=1ore FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ore OCA], [https://pdbe.org/1ore PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ore RCSB], [https://www.ebi.ac.uk/pdbsum/1ore PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ore ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1ore FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ore OCA], [~~http~~://pdbe.org/1ore PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1ore RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1ore PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1ore ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/APT_HUMAN APT_HUMAN]] Defects in APRT are the cause of adenine phosphoribosyltransferase deficiency (APRTD) [MIM:[~~http~~://omim.org/entry/614723 614723]]; also known as 2,8-dihydroxyadenine urolithiasis. An enzymatic deficiency that can lead to urolithiasis and renal failure. Patients have 2,8-dihydroxyadenine (DHA) urinary stones.<ref>PMID:1746557</ref> <ref>PMID:7915931</ref> <ref>PMID:3680503</ref> <ref>PMID:3343350</ref> <ref>PMID:1353080</ref> <ref>PMID:11243733</ref> <ref>PMID:15571218</ref> <ref>PMID:21635362</ref>	+	[https://www.uniprot.org/uniprot/APT_HUMAN APT_HUMAN] Defects in APRT are the cause of adenine phosphoribosyltransferase deficiency (APRTD) [MIM:[https://omim.org/entry/614723 614723]; also known as 2,8-dihydroxyadenine urolithiasis. An enzymatic deficiency that can lead to urolithiasis and renal failure. Patients have 2,8-dihydroxyadenine (DHA) urinary stones.<ref>PMID:1746557</ref> <ref>PMID:7915931</ref> <ref>PMID:3680503</ref> <ref>PMID:3343350</ref> <ref>PMID:1353080</ref> <ref>PMID:11243733</ref> <ref>PMID:15571218</ref> <ref>PMID:21635362</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/APT_HUMAN APT_HUMAN]] Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	+	[https://www.uniprot.org/uniprot/APT_HUMAN APT_HUMAN] Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ore 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=1ore ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	In mammals, adenine phosphoribosyltransferase (APRT, EC 2.4.2.7) is present in all tissues and provides the only known mechanism for the metabolic salvage of adenine resulting from the polyamine biosynthesis pathway or from dietary sources. In humans, APRT deficiency results in serious kidney illness such as nephrolithiasis, interstitial nephritis, and chronic renal failure as a result of 2,8-dihydroxyadenine (DHA) precipitation in the renal interstitium. To address the molecular basis of DHA-urolithiasis, the recombinant human APRT was crystallized in complex with adenosine 5'-monophosphate (AMP). Refinement of X-ray diffraction data extended to 2.1 A resolution led to a final crystallographic R(factor) of 13.3% and an R(free) of 17.6%. This structure is composed of nine beta-strands and six alpha-helices, and the active site pocket opens slightly to accommodate the AMP product. The core of APRT is similar to that of other phosphoribosyltransferases (PRTases), although the adenine-binding domain is quite different. Structural comparisons between the human APRT and other "type I" PRTases of known structure revealed several important features of the biochemistry of PRTases. We propose that the residues located at positions corresponding to Leu159 and Ala131 in hAPRT are responsible for the base specificities of type I PRTases. The comparative analysis shown here also provides structural information for the mechanism by which mutations in the human APRT lead to DHA-urolithiasis.
-
-	Three-dimensional structure of human adenine phosphoribosyltransferase and its relation to DHA-urolithiasis.,Silva M, Silva CH, Iulek J, Thiemann OH Biochemistry. 2004 Jun 22;43(24):7663-71. PMID:15196008<ref>PMID:15196008</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1ore" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 39:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Adenine phosphoribosyltransferase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Iulek, J]]	+	[[Category: Iulek J]]
-	[[Category: Oliva, G]]	+	[[Category: Oliva G]]
-	[[Category: Silva~~, C H.T P~~]]	+	[[Category: Silva CHTP]]
-	[[Category: Silva, M]]	+	[[Category: Silva M]]
-	[[Category: Thiemann~~, O H]]~~	+	[[Category: Thiemann OH]]
-	~~[[Category: Glycosyl transferase]]~~	+
-	~~[[Category: Human adenine phosphoribosyltransferase]]~~	+
-	~~[[Category: Leishmaniasis]]~~	+
-	~~[[Category: Purine salvage]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Urolithiasis~~]]	+

OCA at 07:13, 9 December 2020

OCA — Wed, 09 Dec 2020 07:13:55 GMT

←Older revision		Revision as of 07:13, 9 December 2020
Line 1:		Line 1:

	==Human Adenine Phosphoribosyltransferase==		==Human Adenine Phosphoribosyltransferase==
-	<StructureSection load='1ore' size='340' side='right' caption='[[1ore]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='1ore' size='340' side='right'caption='[[1ore]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ore]] is a 1 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=1ORE OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1ORE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ore]] is a 1 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=1ORE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ORE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">APRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">APRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase Adenine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.7 2.4.2.7] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase Adenine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.7 2.4.2.7] </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=1ore FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ore OCA], [http://pdbe.org/1ore PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ore RCSB], [http://www.ebi.ac.uk/pdbsum/1ore PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ore ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ore FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ore OCA], [http://pdbe.org/1ore PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ore RCSB], [http://www.ebi.ac.uk/pdbsum/1ore PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ore ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 17:		Line 17:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/or/1ore_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/or/1ore_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 32:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 1ore" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1ore" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Phosphoribosyltransferase 3D structures\|Phosphoribosyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 38:		Line 41:
	[[Category: Adenine phosphoribosyltransferase]]		[[Category: Adenine phosphoribosyltransferase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Iulek, J]]		[[Category: Iulek, J]]
	[[Category: Oliva, G]]		[[Category: Oliva, G]]

OCA at 09:06, 12 October 2017

OCA — Thu, 12 Oct 2017 09:06:33 GMT

←Older revision		Revision as of 09:06, 12 October 2017
Line 1:		Line 1:
		+
	==Human Adenine Phosphoribosyltransferase==		==Human Adenine Phosphoribosyltransferase==
	<StructureSection load='1ore' size='340' side='right' caption='[[1ore]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1ore' size='340' side='right' caption='[[1ore]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">APRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">APRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase Adenine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.7 2.4.2.7] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase Adenine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.7 2.4.2.7] </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=1ore FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ore OCA], [http://pdbe.org/1ore PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ore RCSB], [http://www.ebi.ac.uk/pdbsum/1ore 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=1ore FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ore OCA], [http://pdbe.org/1ore PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ore RCSB], [http://www.ebi.ac.uk/pdbsum/1ore PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ore ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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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=1ore ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 31:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 1ore" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1ore" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Phosphoribosyltransferase\|Phosphoribosyltransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:51, 11 September 2015

OCA — Fri, 11 Sep 2015 07:51:04 GMT

←Older revision		Revision as of 07:51, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1ore' size='340' side='right' caption='[[1ore]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1ore' size='340' side='right' caption='[[1ore]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ore]] is a 1 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=1ORE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ORE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ore]] is a 1 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=1ORE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ORE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">APRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">APRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase Adenine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.7 2.4.2.7] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase Adenine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.7 2.4.2.7] </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=1ore FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ore OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ore RCSB], [http://www.ebi.ac.uk/pdbsum/1ore 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=1ore FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ore OCA], [http://pdbe.org/1ore PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ore RCSB], [http://www.ebi.ac.uk/pdbsum/1ore PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 30:		Line 30:
	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 1ore" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Adenine phosphoribosyltransferase]]		[[Category: Adenine phosphoribosyltransferase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Iulek, J]]		[[Category: Iulek, J]]
	[[Category: Oliva, G]]		[[Category: Oliva, G]]

OCA at 07:10, 6 January 2015

OCA — Tue, 06 Jan 2015 07:10:51 GMT

←Older revision		Revision as of 07:10, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ore]] is a 1 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=1ORE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ORE FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ore]] is a 1 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=1ORE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ORE FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">APRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">APRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase Adenine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.7 2.4.2.7] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase Adenine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.7 2.4.2.7] </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=1ore FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ore OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ore RCSB], [http://www.ebi.ac.uk/pdbsum/1ore 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=1ore FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ore OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ore RCSB], [http://www.ebi.ac.uk/pdbsum/1ore PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/APT_HUMAN APT_HUMAN]] Defects in APRT are the cause of adenine phosphoribosyltransferase deficiency (APRTD) [MIM:[http://omim.org/entry/614723 614723]]; also known as 2,8-dihydroxyadenine urolithiasis. An enzymatic deficiency that can lead to urolithiasis and renal failure. Patients have 2,8-dihydroxyadenine (DHA) urinary stones.<ref>PMID:1746557</ref> <ref>PMID:7915931</ref> <ref>PMID:3680503</ref> <ref>PMID:3343350</ref> <ref>PMID:1353080</ref> <ref>PMID:11243733</ref> <ref>PMID:15571218</ref> <ref>PMID:21635362</ref>		[[http://www.uniprot.org/uniprot/APT_HUMAN APT_HUMAN]] Defects in APRT are the cause of adenine phosphoribosyltransferase deficiency (APRTD) [MIM:[http://omim.org/entry/614723 614723]]; also known as 2,8-dihydroxyadenine urolithiasis. An enzymatic deficiency that can lead to urolithiasis and renal failure. Patients have 2,8-dihydroxyadenine (DHA) urinary stones.<ref>PMID:1746557</ref> <ref>PMID:7915931</ref> <ref>PMID:3680503</ref> <ref>PMID:3343350</ref> <ref>PMID:1353080</ref> <ref>PMID:11243733</ref> <ref>PMID:15571218</ref> <ref>PMID:21635362</ref>
Line 39:		Line 39:
	[[Category: Adenine phosphoribosyltransferase]]		[[Category: Adenine phosphoribosyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Iulek, J.]]	+	[[Category: Iulek, J]]
-	[[Category: Oliva, G.]]	+	[[Category: Oliva, G]]
-	[[Category: Silva, C H.T P.]]	+	[[Category: Silva, C H.T P]]
-	[[Category: Silva, M.]]	+	[[Category: Silva, M]]
-	[[Category: Thiemann, O H.]]	+	[[Category: Thiemann, O H]]
	[[Category: Glycosyl transferase]]		[[Category: Glycosyl transferase]]
	[[Category: Human adenine phosphoribosyltransferase]]		[[Category: Human adenine phosphoribosyltransferase]]

OCA at 16:04, 29 September 2014

OCA — Mon, 29 Sep 2014 16:04:01 GMT

←Older revision		Revision as of 16:04, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1ore~~\| ~~PDB~~=1ore \| ~~SCENE~~= }}	+	==Human Adenine Phosphoribosyltransferase==
-	===~~Human~~ Adenine ~~Phosphoribosyltransferase~~===	+	<StructureSection load='1ore' size='340' side='right' caption='[[1ore]], [[Resolution\|resolution]] 2.10Å' scene=''>
-	~~{{ABSTRACT_PUBMED_15196008}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1ore]] is a 1 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=1ORE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ORE FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">APRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase Adenine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.7 2.4.2.7] </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=1ore FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ore OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ore RCSB], [http://www.ebi.ac.uk/pdbsum/1ore PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/APT_HUMAN APT_HUMAN]] Defects in APRT are the cause of adenine phosphoribosyltransferase deficiency (APRTD) [MIM:[http://omim.org/entry/614723 614723]]; also known as 2,8-dihydroxyadenine urolithiasis. An enzymatic deficiency that can lead to urolithiasis and renal failure. Patients have 2,8-dihydroxyadenine (DHA) urinary stones.<ref>PMID:1746557</ref> <ref>PMID:7915931</ref> <ref>PMID:3680503</ref> <ref>PMID:3343350</ref> <ref>PMID:1353080</ref> <ref>PMID:11243733</ref> <ref>PMID:15571218</ref> <ref>PMID:21635362</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/APT_HUMAN APT_HUMAN]] Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
		+	== 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/or/1ore_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 mammals, adenine phosphoribosyltransferase (APRT, EC 2.4.2.7) is present in all tissues and provides the only known mechanism for the metabolic salvage of adenine resulting from the polyamine biosynthesis pathway or from dietary sources. In humans, APRT deficiency results in serious kidney illness such as nephrolithiasis, interstitial nephritis, and chronic renal failure as a result of 2,8-dihydroxyadenine (DHA) precipitation in the renal interstitium. To address the molecular basis of DHA-urolithiasis, the recombinant human APRT was crystallized in complex with adenosine 5'-monophosphate (AMP). Refinement of X-ray diffraction data extended to 2.1 A resolution led to a final crystallographic R(factor) of 13.3% and an R(free) of 17.6%. This structure is composed of nine beta-strands and six alpha-helices, and the active site pocket opens slightly to accommodate the AMP product. The core of APRT is similar to that of other phosphoribosyltransferases (PRTases), although the adenine-binding domain is quite different. Structural comparisons between the human APRT and other "type I" PRTases of known structure revealed several important features of the biochemistry of PRTases. We propose that the residues located at positions corresponding to Leu159 and Ala131 in hAPRT are responsible for the base specificities of type I PRTases. The comparative analysis shown here also provides structural information for the mechanism by which mutations in the human APRT lead to DHA-urolithiasis.

-	~~==Disease==~~	+	Three-dimensional structure of human adenine phosphoribosyltransferase and its relation to DHA-urolithiasis.,Silva M, Silva CH, Iulek J, Thiemann OH Biochemistry. 2004 Jun 22;43(24):7663-71. PMID:15196008<ref>PMID:15196008</ref>
-	~~[[http://www.uniprot.org/uniprot/APT_HUMAN APT_HUMAN]] Defects in APRT are the cause~~ of adenine phosphoribosyltransferase ~~deficiency (APRTD) [MIM:[http://omim.org/entry/614723 614723]]; also known as 2,8~~-~~dihydroxyadenine~~ urolithiasis. ~~An enzymatic deficiency that can lead to urolithiasis and renal failure~~. ~~Patients have 2,8-dihydroxyadenine~~ (~~DHA~~) ~~urinary stones~~.~~<ref>~~PMID:~~1746557</ref><ref>PMID:7915931</ref><ref>PMID:3680503</ref><ref>PMID:3343350</ref><ref>PMID:1353080</ref><ref>PMID:11243733</ref><ref>PMID:15571218</ref>~~<ref>PMID:~~21635362~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www~~.~~uniprot~~.~~org/uniprot/APT_HUMAN APT_HUMAN]] Catalyzes a salvage reaction resulting in the formation~~ of ~~AMP, that is energically less costly than de novo synthesis~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[1ore]] is a 1 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=1ORE OCA].~~	+

	==See Also==		==See Also==
	*[[Phosphoribosyltransferase\|Phosphoribosyltransferase]]		*[[Phosphoribosyltransferase\|Phosphoribosyltransferase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:015196008</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Adenine phosphoribosyltransferase]]		[[Category: Adenine phosphoribosyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 03:44, 25 March 2013

OCA — Mon, 25 Mar 2013 03:44:23 GMT

←Older revision		Revision as of 03:44, 25 March 2013
Line 1:		Line 1:
-	[[Image:1ore.png\|left\|200px]]
-
	{{STRUCTURE_1ore\| PDB=1ore \| SCENE= }}		{{STRUCTURE_1ore\| PDB=1ore \| SCENE= }}
-
	===Human Adenine Phosphoribosyltransferase===		===Human Adenine Phosphoribosyltransferase===
-
	{{ABSTRACT_PUBMED_15196008}}		{{ABSTRACT_PUBMED_15196008}}
		+
		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/APT_HUMAN APT_HUMAN]] Defects in APRT are the cause of adenine phosphoribosyltransferase deficiency (APRTD) [MIM:[http://omim.org/entry/614723 614723]]; also known as 2,8-dihydroxyadenine urolithiasis. An enzymatic deficiency that can lead to urolithiasis and renal failure. Patients have 2,8-dihydroxyadenine (DHA) urinary stones.<ref>PMID:1746557</ref><ref>PMID:7915931</ref><ref>PMID:3680503</ref><ref>PMID:3343350</ref><ref>PMID:1353080</ref><ref>PMID:11243733</ref><ref>PMID:15571218</ref><ref>PMID:21635362</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/APT_HUMAN APT_HUMAN]] Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.

	==About this Structure==		==About this Structure==
	[[1ore]] is a 1 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=1ORE OCA].		[[1ore]] is a 1 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=1ORE OCA].
		+
		+	==See Also==
		+	*[[Phosphoribosyltransferase\|Phosphoribosyltransferase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:015196008</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015196008</ref><references group="xtra"/><references/>
	[[Category: Adenine phosphoribosyltransferase]]		[[Category: Adenine phosphoribosyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

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

OCA — Wed, 12 Dec 2012 21:41:45 GMT

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

←Older revision

Revision as of 21:41, 12 December 2012

OCA at 21:41, 12 December 2012

OCA — Wed, 12 Dec 2012 21:41:42 GMT

←Older revision		Revision as of 21:41, 12 December 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1ore.png\|left\|200px]]		[[Image:1ore.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1ore", 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_1ore\| PDB=1ore \| SCENE= }}		{{STRUCTURE_1ore\| PDB=1ore \| SCENE= }}

	===Human Adenine Phosphoribosyltransferase===		===Human Adenine Phosphoribosyltransferase===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15196008}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15196008 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_15196008}}		{{ABSTRACT_PUBMED_15196008}}
-
-	==Disease==
-	Known disease associated with this structure: Urolithiasis, 2,8-dihydroxyadenine OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=102600 102600]]

	==About this Structure==		==About this Structure==
-	~~1ORE~~ is a 1 chain structure of 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=1ORE OCA].	+	[[1ore]] is a 1 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=1ORE OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15196008~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015196008</ref><references group="xtra"/>
	[[Category: Adenine phosphoribosyltransferase]]		[[Category: Adenine phosphoribosyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 38:		Line 23:
	[[Category: Leishmaniasis]]		[[Category: Leishmaniasis]]
	[[Category: Purine salvage]]		[[Category: Purine salvage]]
		+	[[Category: Transferase]]
	[[Category: Urolithiasis]]		[[Category: Urolithiasis]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:25:47 2009''

OCA at 15:25, 17 February 2009

OCA — Tue, 17 Feb 2009 15:25:48 GMT

←Older revision		Revision as of 15:25, 17 February 2009
Line 23:		Line 23:

	==About this Structure==		==About this Structure==
-	1ORE is a ~~[[Single protein]]~~ structure of 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=1ORE OCA].	+	1ORE is a 1 chain structure of 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=1ORE OCA].

	==Reference==		==Reference==
-	~~Three-dimensional structure of human adenine phosphoribosyltransferase and its relation to DHA-urolithiasis., Silva M, Silva CH, Iulek J, Thiemann OH, Biochemistry. 2004 Jun 22;43(24):7663-71.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/15196008 15196008]~~	+	<ref group="xtra">PMID:15196008</ref><references group="xtra"/>
	[[Category: Adenine phosphoribosyltransferase]]		[[Category: Adenine phosphoribosyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Single protein]]
	[[Category: Iulek, J.]]		[[Category: Iulek, J.]]
	[[Category: Oliva, G.]]		[[Category: Oliva, G.]]
Line 41:		Line 40:
	[[Category: Urolithiasis]]		[[Category: Urolithiasis]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue ~~Jul 29 00~~:23:~~59 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:25:47 2009''