5f7x - Revision history

OCA at 06:41, 19 July 2023

2023-07-19T06:41:37Z

←Older revision		Revision as of 06:41, 19 July 2023
Line 3:		Line 3:
	<StructureSection load='5f7x' size='340' side='right'caption='[[5f7x]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='5f7x' size='340' side='right'caption='[[5f7x]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5f7x]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Blood_fluke Blood fluke~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F7X OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5F7X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5f7x]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F7X FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=SO4:SULFATE+ION'>SO4</scene~~>, ~~<scene name='pdbligand=TBN:2-(4-AMINO-PYRROLO~~[~~2,3-D~~]~~PYRIMIDIN-7-YL)-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL'>TBN</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]] 1.77Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[4l6i\|4l6i]], [[4l5a\|4l5a]], [[4l5c\|4l5c]], [[4l5y\|4l5y]], [[5f73\|5f73]], [[5f76\|5f76]], [[5f77\|5f77]], [[5f78\|5f78]], [[5f7j\|5f7j]], [[5f7o\|5f7o]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TBN:2-(4-AMINO-PYRROLO[2,3-D]PYRIMIDIN-7-YL)-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL'>TBN</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f7x OCA], [https://pdbe.org/5f7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f7x RCSB], [https://www.ebi.ac.uk/pdbsum/5f7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f7x ProSAT]</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=5f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f7x OCA], [~~http~~://pdbe.org/5f7x PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5f7x RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5f7x PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5f7x ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/I0B503_SCHMA I0B503_SCHMA]] 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 (By similarity).[HAMAP-Rule:MF_03155]	+	[https://www.uniprot.org/uniprot/I0B503_SCHMA I0B503_SCHMA] 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 (By similarity).[HAMAP-Rule:MF_03155]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Blood fluke]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~S-methyl-5'-thioadenosine phosphorylase~~]]	+	[[Category: Schistosoma mansoni]]
-	[[Category: Brandao-Neto, J]]	+	[[Category: Brandao-Neto J]]
-	[[Category: DeMarco, R]]	+	[[Category: DeMarco R]]
-	[[Category: Pereira~~, H M~~]]	+	[[Category: Pereira HM]]
-	[[Category: Torini~~, J R]]~~	+	[[Category: Torini JR]]
-	~~[[Category: Transferase~~]]	+

OCA at 06:22, 17 April 2019

2019-04-17T06:22:14Z

←Older revision		Revision as of 06:22, 17 April 2019
Line 1:		Line 1:

	==Crystal structure of Mutant Q289L of adenosine/Methylthioadenosine phosphorylase from Schistosoma mansoni in complex with Tubercidin==		==Crystal structure of Mutant Q289L of adenosine/Methylthioadenosine phosphorylase from Schistosoma mansoni in complex with Tubercidin==
-	<StructureSection load='5f7x' size='340' side='right' caption='[[5f7x]], [[Resolution\|resolution]] 1.77Å' scene=''>	+	<StructureSection load='5f7x' size='340' side='right'caption='[[5f7x]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5f7x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F7X FirstGlance]. <br>		<table><tr><td colspan='2'>[[5f7x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F7X FirstGlance]. <br>
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Blood fluke]]		[[Category: Blood fluke]]
		+	[[Category: Large Structures]]
	[[Category: S-methyl-5'-thioadenosine phosphorylase]]		[[Category: S-methyl-5'-thioadenosine phosphorylase]]
	[[Category: Brandao-Neto, J]]		[[Category: Brandao-Neto, J]]

OCA at 12:41, 6 November 2017

2017-11-06T12:41:36Z

←Older revision		Revision as of 12:41, 6 November 2017
Line 3:		Line 3:
	<StructureSection load='5f7x' size='340' side='right' caption='[[5f7x]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='5f7x' size='340' side='right' caption='[[5f7x]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5f7x]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F7X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5f7x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F7X FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TBN:2-(4-AMINO-PYRROLO[2,3-D]PYRIMIDIN-7-YL)-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL'>TBN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TBN:2-(4-AMINO-PYRROLO[2,3-D]PYRIMIDIN-7-YL)-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL'>TBN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l6i\|4l6i]], [[4l5a\|4l5a]], [[4l5c\|4l5c]], [[4l5y\|4l5y]], [[5f73\|5f73]], [[5f76\|5f76]], [[5f77\|5f77]], [[5f78\|5f78]], [[5f7j\|5f7j]], [[5f7o\|5f7o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l6i\|4l6i]], [[4l5a\|4l5a]], [[4l5c\|4l5c]], [[4l5y\|4l5y]], [[5f73\|5f73]], [[5f76\|5f76]], [[5f77\|5f77]], [[5f78\|5f78]], [[5f7j\|5f7j]], [[5f7o\|5f7o]]</td></tr>
Line 24:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Blood fluke]]
	[[Category: S-methyl-5'-thioadenosine phosphorylase]]		[[Category: S-methyl-5'-thioadenosine phosphorylase]]
	[[Category: Brandao-Neto, J]]		[[Category: Brandao-Neto, J]]

OCA at 14:56, 22 December 2016

2016-12-22T14:56:02Z

←Older revision		Revision as of 14:56, 22 December 2016
Line 11:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/I0B503_SCHMA I0B503_SCHMA]] 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 (By similarity).[HAMAP-Rule:MF_03155]		[[http://www.uniprot.org/uniprot/I0B503_SCHMA I0B503_SCHMA]] 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 (By similarity).[HAMAP-Rule:MF_03155]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Schistosoma mansoni do not have de novo purine pathways and rely on purine salvage for their purine supply. It has been demonstrated that, unlike humans, the S. mansoni is able to produce adenine directly from adenosine, although the enzyme responsible for this activity was unknown. In the present work we show that S. mansoni 5 -deoxy-5 -methylthioadenosine phosphorylase (MTAP, E.C. 2.4.2.28) is capable of use adenosine as a substrate to the production of adenine. Through kinetics assays, we show that the Schistosoma mansoni MTAP (SmMTAP), unlike the mammalian MTAP, uses adenosine substrate with the same efficiency as MTA phosphorolysis, which suggests that this enzyme is part of the purine pathway salvage in S. mansoni and could be a promising target for anti-schistosoma therapies. Here, we present 13 SmMTAP structures from the wild type (WT), including three single and one double mutant, and generate a solid structural framework for structure description. These crystal structures of SmMTAP reveal that the active site contains three substitutions within and near the active site when compared to it mammalian counterpart, thus opening up the possibility of developing specific inhibitors to the parasite MTAP. The structural and kinetic data for 5 substrates reveal the structural basis for this interaction, providing substract for inteligent design of new compounds for block this enzyme activity.
		+
		+	Crystal Structure of Schistosoma mansoni Adenosine Phosphorylase/5'-Methylthioadenosine Phosphorylase and Its Importance on Adenosine Salvage Pathway.,Torini JR, Brandao-Neto J, DeMarco R, Pereira HD PLoS Negl Trop Dis. 2016 Dec 9;10(12):e0005178. doi:, 10.1371/journal.pntd.0005178. eCollection 2016 Dec. PMID:27935959<ref>PMID:27935959</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5f7x" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 19:14, 15 December 2016

2016-12-15T19:14:05Z

←Older revision		Revision as of 19:14, 15 December 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5f7x is ~~ON HOLD until Dec 08 2017~~	+	==Crystal structure of Mutant Q289L of adenosine/Methylthioadenosine phosphorylase from Schistosoma mansoni in complex with Tubercidin==
-		+	<StructureSection load='5f7x' size='340' side='right' caption='[[5f7x]], [[Resolution\|resolution]] 1.77Å' scene=''>
-	~~Authors~~: ~~Torini~~, J.R., ~~Brandao~~-~~Neto~~, J., ~~DeMarco~~, R., ~~Pereira~~, H.M.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5f7x]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F7X FirstGlance]. <br>
-	~~Description~~: ~~Crystal structure~~ of ~~Mutant Q289L~~ of ~~adenosine/Methylthioadenosine phosphorylase from Schistosoma mansoni~~ in ~~complex~~ with ~~Tubercidin~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TBN:2-(4-AMINO-PYRROLO[2,3-D]PYRIMIDIN-7-YL)-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL'>TBN</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l6i\|4l6i]], [[4l5a\|4l5a]], [[4l5c\|4l5c]], [[4l5y\|4l5y]], [[5f73\|5f73]], [[5f76\|5f76]], [[5f77\|5f77]], [[5f78\|5f78]], [[5f7j\|5f7j]], [[5f7o\|5f7o]]</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=5f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f7x OCA], [http://pdbe.org/5f7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f7x RCSB], [http://www.ebi.ac.uk/pdbsum/5f7x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f7x ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/I0B503_SCHMA I0B503_SCHMA]] 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 (By similarity).[HAMAP-Rule:MF_03155]
		+	__TOC__
		+	</StructureSection>
		+	[[Category: S-methyl-5'-thioadenosine phosphorylase]]
	[[Category: Brandao-Neto, J]]		[[Category: Brandao-Neto, J]]
-	[[Category: ~~Pereira~~, ~~H.M~~]]	+	[[Category: DeMarco, R]]
-	[[Category: ~~Demarco~~, R]]	+	[[Category: Pereira, H M]]
-	[[Category: Torini, J.R]]	+	[[Category: Torini, J R]]
		+	[[Category: Transferase]]

OCA at 17:37, 30 December 2015

2015-12-30T17:37:12Z

←Older revision		Revision as of 17:37, 30 December 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5f7x is ON HOLD	+	The entry 5f7x is ON HOLD until Dec 08 2017

-	Authors: Torini, J.R, Brandao-Neto, J., DeMarco, R., Pereira, H.M.	+	Authors: Torini, J.R., Brandao-Neto, J., DeMarco, R., Pereira, H.M.

	Description: Crystal structure of Mutant Q289L of adenosine/Methylthioadenosine phosphorylase from Schistosoma mansoni in complex with Tubercidin		Description: Crystal structure of Mutant Q289L of adenosine/Methylthioadenosine phosphorylase from Schistosoma mansoni in complex with Tubercidin
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
		+	[[Category: Brandao-Neto, J]]
	[[Category: Pereira, H.M]]		[[Category: Pereira, H.M]]
-	[[Category: Torini, J.R, Brandao-Neto, J]]
	[[Category: Demarco, R]]		[[Category: Demarco, R]]
		+	[[Category: Torini, J.R]]

OCA: Protected "5f7x" [edit=sysop:move=sysop]

2015-12-16T12:40:44Z

Protected "5f7x" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:40, 16 December 2015

OCA: New page: '''Unreleased structure''' The entry 5f7x is ON HOLD Authors: Torini, J.R, Brandao-Neto, J., DeMarco, R., Pereira, H.M. Description: Crystal structure of Mutant Q289L of adenosine/Meth...

2015-12-16T12:40:42Z

New page: '''Unreleased structure''' The entry 5f7x is ON HOLD Authors: Torini, J.R, Brandao-Neto, J., DeMarco, R., Pereira, H.M. Description: Crystal structure of Mutant Q289L of adenosine/Meth...

New page

'''Unreleased structure'''

The entry 5f7x is ON HOLD

Authors: Torini, J.R, Brandao-Neto, J., DeMarco, R., Pereira, H.M.

Description: Crystal structure of Mutant Q289L of adenosine/Methylthioadenosine phosphorylase from Schistosoma mansoni in complex with Tubercidin
[[Category: Unreleased Structures]]
[[Category: Pereira, H.M]]
[[Category: Torini, J.R, Brandao-Neto, J]]
[[Category: Demarco, R]]