3oze - Revision history

OCA at 10:37, 21 February 2024

OCA — Wed, 21 Feb 2024 10:37:40 GMT

←Older revision		Revision as of 10:37, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='3oze' size='340' side='right'caption='[[3oze]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3oze' size='340' side='right'caption='[[3oze]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3oze]] is a 6 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=3OZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OZE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3oze]] is a 6 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=3OZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OZE 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></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]] 2Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max~~-~~height: 3em;'>[[3ozc\|3ozc]]~~, [[~~3ozd~~\|~~3ozd~~]]~~</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></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>MTAP, MSAP ([https://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~~'>[https://en.wikipedia.org/wiki/S-methyl-5'-thioadenosine_phosphorylase S-methyl-5'-thioadenosine phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.28 2.4.2.28] </~~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=3oze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oze OCA], [https://pdbe.org/3oze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oze RCSB], [https://www.ebi.ac.uk/pdbsum/3oze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oze 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=3oze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oze OCA], [https://pdbe.org/3oze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oze RCSB], [https://www.ebi.ac.uk/pdbsum/3oze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oze ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Defects in MTAP are the cause of diaphyseal medullary stenosis with malignant fibrous histiocytoma (DMSMFH) [MIM:[https://omim.org/entry/112250 112250]]. An autosomal dominant bone dysplasia characterized by pathologic fractures due to abnormal cortical growth and diaphyseal medullary stenosis. The fractures heal poorly, and there is progressive bowing of the lower extremities. Some patients show a limb-girdle myopathy, with muscle weakness and atrophy. Approximately 35% of affected individuals develop an aggressive form of bone sarcoma consistent with malignant fibrous histiocytoma or osteosarcoma. Note=DMSMFH causing mutations found in MTAP exon 9 result in exon skipping and dysregulated alternative splicing of all MTAP isoforms (PubMed:22464254).<ref>PMID:22464254</ref> Note=Loss of MTAP activity may play a role in human cancer. MTAP loss has been reported in a number of cancers, including osteosarcoma, malignant melanoma and gastric cancer.[HAMAP-Rule:MF_03155]	+	[https://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN] Defects in MTAP are the cause of diaphyseal medullary stenosis with malignant fibrous histiocytoma (DMSMFH) [MIM:[https://omim.org/entry/112250 112250]. An autosomal dominant bone dysplasia characterized by pathologic fractures due to abnormal cortical growth and diaphyseal medullary stenosis. The fractures heal poorly, and there is progressive bowing of the lower extremities. Some patients show a limb-girdle myopathy, with muscle weakness and atrophy. Approximately 35% of affected individuals develop an aggressive form of bone sarcoma consistent with malignant fibrous histiocytoma or osteosarcoma. Note=DMSMFH causing mutations found in MTAP exon 9 result in exon skipping and dysregulated alternative splicing of all MTAP isoforms (PubMed:22464254).<ref>PMID:22464254</ref> Note=Loss of MTAP activity may play a role in human cancer. MTAP loss has been reported in a number of cancers, including osteosarcoma, malignant melanoma and gastric cancer.[HAMAP-Rule:MF_03155]
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.<ref>PMID:3091600</ref>	+	[https://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN] Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.<ref>PMID:3091600</ref>

	==See Also==		==See Also==
Line 21:		Line 19:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: S-methyl-5'-thioadenosine phosphorylase]]~~	+	[[Category: Almo SC]]
-	[[Category: Almo~~, S C~~]]	+	[[Category: Guan R]]
-	[[Category: Guan, R]]	+	[[Category: Ho M]]
-	[[Category: Ho, M]]	+	[[Category: Schramm VL]]
-	[[Category: Schramm~~, V L]]~~	+
-	~~[[Category: 5'-methylthioadenosine]]~~	+
-	~~[[Category: Mtap]]~~	+
-	~~[[Category: Phosphorylase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 11:04, 18 May 2022

OCA — Wed, 18 May 2022 11:04:44 GMT

←Older revision		Revision as of 11:04, 18 May 2022
Line 1:		Line 1:

	==Crystal Structure of human 5'-deoxy-5'-methyladenosine phosphorylase==		==Crystal Structure of human 5'-deoxy-5'-methyladenosine phosphorylase==
-	<StructureSection load='3oze' size='340' side='right' caption='[[3oze]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='3oze' size='340' side='right'caption='[[3oze]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3oze]] is a 6 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=3OZE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3OZE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3oze]] is a 6 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=3OZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OZE 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></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></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ozc\|3ozc]], [[3ozd\|3ozd]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ozc\|3ozc]], [[3ozd\|3ozd]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MTAP, MSAP ([~~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">MTAP, MSAP ([https://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/S-methyl-5'-thioadenosine_phosphorylase S-methyl-5'-thioadenosine phosphorylase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.28 2.4.2.28] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/S-methyl-5'-thioadenosine_phosphorylase S-methyl-5'-thioadenosine phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.28 2.4.2.28] </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=3oze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oze OCA], [~~http~~://pdbe.org/3oze PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3oze RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3oze PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3oze 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=3oze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oze OCA], [https://pdbe.org/3oze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oze RCSB], [https://www.ebi.ac.uk/pdbsum/3oze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oze ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Defects in MTAP are the cause of diaphyseal medullary stenosis with malignant fibrous histiocytoma (DMSMFH) [MIM:[~~http~~://omim.org/entry/112250 112250]]. An autosomal dominant bone dysplasia characterized by pathologic fractures due to abnormal cortical growth and diaphyseal medullary stenosis. The fractures heal poorly, and there is progressive bowing of the lower extremities. Some patients show a limb-girdle myopathy, with muscle weakness and atrophy. Approximately 35% of affected individuals develop an aggressive form of bone sarcoma consistent with malignant fibrous histiocytoma or osteosarcoma. Note=DMSMFH causing mutations found in MTAP exon 9 result in exon skipping and dysregulated alternative splicing of all MTAP isoforms (PubMed:22464254).<ref>PMID:22464254</ref> Note=Loss of MTAP activity may play a role in human cancer. MTAP loss has been reported in a number of cancers, including osteosarcoma, malignant melanoma and gastric cancer.[HAMAP-Rule:MF_03155]	+	[[https://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Defects in MTAP are the cause of diaphyseal medullary stenosis with malignant fibrous histiocytoma (DMSMFH) [MIM:[https://omim.org/entry/112250 112250]]. An autosomal dominant bone dysplasia characterized by pathologic fractures due to abnormal cortical growth and diaphyseal medullary stenosis. The fractures heal poorly, and there is progressive bowing of the lower extremities. Some patients show a limb-girdle myopathy, with muscle weakness and atrophy. Approximately 35% of affected individuals develop an aggressive form of bone sarcoma consistent with malignant fibrous histiocytoma or osteosarcoma. Note=DMSMFH causing mutations found in MTAP exon 9 result in exon skipping and dysregulated alternative splicing of all MTAP isoforms (PubMed:22464254).<ref>PMID:22464254</ref> Note=Loss of MTAP activity may play a role in human cancer. MTAP loss has been reported in a number of cancers, including osteosarcoma, malignant melanoma and gastric cancer.[HAMAP-Rule:MF_03155]
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.<ref>PMID:3091600</ref>	+	[[https://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.<ref>PMID:3091600</ref>
		+
		+	==See Also==
		+	*[[5'-deoxy-5'-methylthioadenosine phosphorylase 3D structures\|5'-deoxy-5'-methylthioadenosine phosphorylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 19:		Line 22:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: S-methyl-5'-thioadenosine phosphorylase]]		[[Category: S-methyl-5'-thioadenosine phosphorylase]]
	[[Category: Almo, S C]]		[[Category: Almo, S C]]

OCA at 08:52, 8 November 2017

OCA — Wed, 08 Nov 2017 08:52:34 GMT

←Older revision		Revision as of 08:52, 8 November 2017
Line 14:		Line 14:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.<ref>PMID:3091600</ref>		[[http://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.<ref>PMID:3091600</ref>
-
-	==See Also==
-	*[[5'-deoxy-5'-methylthioadenosine phosphorylase\|5'-deoxy-5'-methylthioadenosine phosphorylase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:35, 11 August 2016

OCA — Thu, 11 Aug 2016 14:35:55 GMT

←Older revision		Revision as of 14:35, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of human 5'-deoxy-5'-methyladenosine phosphorylase==		==Crystal Structure of human 5'-deoxy-5'-methyladenosine phosphorylase==
	<StructureSection load='3oze' size='340' side='right' caption='[[3oze]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3oze' size='340' side='right' caption='[[3oze]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3oze]] is a 6 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=3OZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OZE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3oze]] is a 6 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=3OZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OZE 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></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></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ozc\|3ozc]], [[3ozd\|3ozd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ozc\|3ozc]], [[3ozd\|3ozd]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MTAP, MSAP ([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">MTAP, MSAP ([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/S-methyl-5'-thioadenosine_phosphorylase S-methyl-5'-thioadenosine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.28 2.4.2.28] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/S-methyl-5'-thioadenosine_phosphorylase S-methyl-5'-thioadenosine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.28 2.4.2.28] </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=3oze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oze OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oze RCSB], [http://www.ebi.ac.uk/pdbsum/3oze 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=3oze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oze OCA], [http://pdbe.org/3oze PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3oze RCSB], [http://www.ebi.ac.uk/pdbsum/3oze PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3oze ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: S-methyl-5'-thioadenosine phosphorylase]]		[[Category: S-methyl-5'-thioadenosine phosphorylase]]
	[[Category: Almo, S C]]		[[Category: Almo, S C]]

OCA at 13:24, 6 November 2014

OCA — Thu, 06 Nov 2014 13:24:50 GMT

←Older revision		Revision as of 13:24, 6 November 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3oze~~\| ~~PDB~~=3oze \| ~~SCENE~~= }}	+	==Crystal Structure of human 5'-deoxy-5'-methyladenosine phosphorylase==
-	===~~Crystal Structure of human~~ 5'-~~deoxy~~-5'-~~methyladenosine~~ phosphorylase===	+	<StructureSection load='3oze' size='340' side='right' caption='[[3oze]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3oze]] is a 6 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=3OZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OZE 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></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ozc\|3ozc]], [[3ozd\|3ozd]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MTAP, MSAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/S-methyl-5'-thioadenosine_phosphorylase S-methyl-5'-thioadenosine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.28 2.4.2.28] </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=3oze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oze OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oze RCSB], [http://www.ebi.ac.uk/pdbsum/3oze PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Defects in MTAP are the cause of diaphyseal medullary stenosis with malignant fibrous histiocytoma (DMSMFH) [MIM:[http://omim.org/entry/112250 112250]]. An autosomal dominant bone dysplasia characterized by pathologic fractures due to abnormal cortical growth and diaphyseal medullary stenosis. The fractures heal poorly, and there is progressive bowing of the lower extremities. Some patients show a limb-girdle myopathy, with muscle weakness and atrophy. Approximately 35% of affected individuals develop an aggressive form of bone sarcoma consistent with malignant fibrous histiocytoma or osteosarcoma. Note=DMSMFH causing mutations found in MTAP exon 9 result in exon skipping and dysregulated alternative splicing of all MTAP isoforms (PubMed:22464254).<ref>PMID:22464254</ref> Note=Loss of MTAP activity may play a role in human cancer. MTAP loss has been reported in a number of cancers, including osteosarcoma, malignant melanoma and gastric cancer.[HAMAP-Rule:MF_03155]
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.<ref>PMID:3091600</ref>

-	==~~Disease~~==	+	==See Also==
-	[[http://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Defects in MTAP are the cause of diaphyseal medullary stenosis with malignant fibrous histiocytoma (DMSMFH) [MIM:[http://omim.org/entry/112250 112250]]. An autosomal dominant bone dysplasia characterized by pathologic fractures due to abnormal cortical growth and diaphyseal medullary stenosis. The fractures heal poorly, and there is progressive bowing of the lower extremities. Some patients show a limb-girdle myopathy, with muscle weakness and atrophy. Approximately 35% of affected individuals develop an aggressive form of bone sarcoma consistent with malignant fibrous histiocytoma or osteosarcoma. Note=DMSMFH causing mutations found in MTAP exon 9 result in exon skipping and dysregulated alternative splicing of all MTAP isoforms (PubMed:22464254).<ref>PMID:22464254</ref> Note=Loss of MTAP activity may play a role in human cancer. MTAP loss has been reported in a number of cancers, including osteosarcoma, malignant melanoma and gastric cancer.[HAMAP-Rule:MF_03155]	+	*[[5'-deoxy-5'-methylthioadenosine phosphorylase\|5'-deoxy-5'-methylthioadenosine phosphorylase]]
-		+	== References ==
-	~~==Function==~~	+	<references/>
-	~~[[http://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Catalyzes the reversible phosphorylation of S-methyl~~-5'-~~thioadenosine (MTA) to adenine and~~ 5-~~methylthioribose~~-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.<ref>PMID:3091600</ref>	+	__TOC__
-		+	</StructureSection>
-	~~==About this Structure==~~	+
-	~~[[3oze~~]] is a 6 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=3OZE OCA].	+
-		+
-	==~~Reference~~==	+
-	<references ~~group="xtra"~~/><~~references~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: S-methyl-5'-thioadenosine phosphorylase]]		[[Category: S-methyl-5'-thioadenosine phosphorylase]]
-	[[Category: Almo, S C.]]	+	[[Category: Almo, S C]]
-	[[Category: Guan, R.]]	+	[[Category: Guan, R]]
-	[[Category: Ho, M.]]	+	[[Category: Ho, M]]
-	[[Category: Schramm, V L.]]	+	[[Category: Schramm, V L]]
	[[Category: 5'-methylthioadenosine]]		[[Category: 5'-methylthioadenosine]]
	[[Category: Mtap]]		[[Category: Mtap]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 23:13, 24 March 2013

OCA — Sun, 24 Mar 2013 23:13:34 GMT

←Older revision		Revision as of 23:13, 24 March 2013
Line 1:		Line 1:
-	[[Image:3oze.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3oze", 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_3oze\| PDB=3oze \| SCENE= }}		{{STRUCTURE_3oze\| PDB=3oze \| SCENE= }}
-
	===Crystal Structure of human 5'-deoxy-5'-methyladenosine phosphorylase===		===Crystal Structure of human 5'-deoxy-5'-methyladenosine phosphorylase===

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Defects in MTAP are the cause of diaphyseal medullary stenosis with malignant fibrous histiocytoma (DMSMFH) [MIM:[http://omim.org/entry/112250 112250]]. An autosomal dominant bone dysplasia characterized by pathologic fractures due to abnormal cortical growth and diaphyseal medullary stenosis. The fractures heal poorly, and there is progressive bowing of the lower extremities. Some patients show a limb-girdle myopathy, with muscle weakness and atrophy. Approximately 35% of affected individuals develop an aggressive form of bone sarcoma consistent with malignant fibrous histiocytoma or osteosarcoma. Note=DMSMFH causing mutations found in MTAP exon 9 result in exon skipping and dysregulated alternative splicing of all MTAP isoforms (PubMed:22464254).<ref>PMID:22464254</ref> Note=Loss of MTAP activity may play a role in human cancer. MTAP loss has been reported in a number of cancers, including osteosarcoma, malignant melanoma and gastric cancer.[HAMAP-Rule:MF_03155]
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/MTAP_HUMAN MTAP_HUMAN]] Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.<ref>PMID:3091600</ref>

	==About this Structure==		==About this Structure==
	[[3oze]] is a 6 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=3OZE OCA].		[[3oze]] is a 6 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=3OZE OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: S-methyl-5'-thioadenosine phosphorylase]]		[[Category: S-methyl-5'-thioadenosine phosphorylase]]

OCA at 05:44, 28 September 2011

OCA — Wed, 28 Sep 2011 05:44:41 GMT

←Older revision		Revision as of 05:44, 28 September 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3oze.jpg\|left\|200px]]

-	The ~~entry 3oze~~ is ~~ON HOLD~~ ~~until Sep 28 2012~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3oze", 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_3oze\| PDB=3oze \| SCENE= }}

-	~~Authors: Ho, M., Guan, R., Almo, S.C., Schramm, V.L.~~	+	===Crystal Structure of human 5'-deoxy-5'-methyladenosine phosphorylase===

-	~~Description: Crystal~~ Structure ~~of human 5'~~-~~deoxy~~-5'-~~methyladenosine~~ phosphorylase	+
		+	==About this Structure==
		+	[[3oze]] is a 6 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=3OZE OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: S-methyl-5'-thioadenosine phosphorylase]]
		+	[[Category: Almo, S C.]]
		+	[[Category: Guan, R.]]
		+	[[Category: Ho, M.]]
		+	[[Category: Schramm, V L.]]
		+	[[Category: 5'-methylthioadenosine]]
		+	[[Category: Mtap]]
		+	[[Category: Phosphorylase]]
		+	[[Category: Transferase]]

OCA at 05:22, 21 September 2011

OCA — Wed, 21 Sep 2011 05:22:25 GMT

←Older revision		Revision as of 05:22, 21 September 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3oze is ON HOLD until ~~Paper Publication~~	+	The entry 3oze is ON HOLD until Sep 28 2012

	Authors: Ho, M., Guan, R., Almo, S.C., Schramm, V.L.		Authors: Ho, M., Guan, R., Almo, S.C., Schramm, V.L.

	Description: Crystal Structure of human 5'-deoxy-5'-methyladenosine phosphorylase		Description: Crystal Structure of human 5'-deoxy-5'-methyladenosine phosphorylase

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

OCA — Wed, 12 Jan 2011 04:47:05 GMT

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

←Older revision

Revision as of 04:47, 12 January 2011

OCA at 04:47, 12 January 2011

OCA — Wed, 12 Jan 2011 04:47:04 GMT

←Older revision		Revision as of 04:47, 12 January 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3oze is ON HOLD	+	The entry 3oze is ON HOLD until Paper Publication

	Authors: Ho, M., Guan, R., Almo, S.C., Schramm, V.L.		Authors: Ho, M., Guan, R., Almo, S.C., Schramm, V.L.

	Description: Crystal Structure of human 5'-deoxy-5'-methyladenosine phosphorylase		Description: Crystal Structure of human 5'-deoxy-5'-methyladenosine phosphorylase
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 6 05:50:11 2010''