5aow - Revision history

OCA: Redirecting to 6bii

2018-01-17T06:42:16Z

Redirecting to 6bii

←Older revision		Revision as of 06:42, 17 January 2018
Line 1:		Line 1:
-		+	#REDIRECT [[6bii]] This PDB entry is obsolete and replaced by 6bii
-	~~==Ternary Crystal Structure of Pyrococcus yayanosii Glyoxylate Hydroxypyruvate Reductase in presence of D-glycerate==~~	+
-	~~<StructureSection load='5aow' size='340' side='right' caption='~~[[~~5aow]], [[Resolution\|resolution]] 2.00Å' scene=''>~~	+
-	~~== Structural highlights ==~~	+
-	~~<table><tr><td colspan='2'>[[5aow~~]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AOW FirstGlance]. <br>	+
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DGY:(2R)-2,3-DIHYDROXYPROPANOIC+ACID'>DGY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>	+
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5aov\|5aov]]</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=5aow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aow OCA], [http://pdbe.org/5aow PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aow RCSB], [http://www.ebi.ac.uk/pdbsum/5aow PDBsum]</span></td></tr>	+
-	~~</table>~~	+
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	~~Glyoxylate accumulation within cells is highly toxic. In humans, it is associated with hyperoxaluria type 2 (PH2) leading to renal failure. The glyoxylate content within cells is regulated~~ by the NADPH/NADH dependent glyoxylate/hydroxypyruvate reductases (GRHPR). These are highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. Despite the determination of high-resolution X-ray structures, the substrate recognition mode of this class of enzymes remains unclear. We determined the structure at 2.0 A resolution of a thermostable GRHPR from Archaea as a ternary complex in the presence of D-glycerate and NADPH. This shows a binding mode conserved between human and archeal enzymes. We also determined the first structure of GRHPR in presence of glyoxylate at 1.40 A resolution. This revealed the pivotal role of Leu53 and Trp138 in substrate trafficking. These residues act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Taken together, these results allowed us to propose a general model for GRHPR mode of action.	+
-		+
-	New insights into the mechanism of substrates trafficking in Glyoxylate/Hydroxypyruvate reductases.,Lassalle L, Engilberge S, Madern D, Vauclare P, Franzetti B, Girard E Sci Rep. 2016 Feb 11;6:20629. doi: 10.1038/srep20629. PMID:26865263<ref>PMID:26865263</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 5aow" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
-	~~__TOC__~~	+
-	~~</StructureSection>~~	+
-	~~[[Category: Girard, E]]~~	+
-	~~[[Category: Lassalle, L]]~~	+
-	~~[[Category: Archaea]]~~	+
-	~~[[Category: D-glycerate]]~~	+
-	~~[[Category: Glyoxylate hydroxypyruvate reductase]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+

OCA at 14:58, 2 March 2016

2016-03-02T14:58:36Z

←Older revision		Revision as of 14:58, 2 March 2016
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-	'''Unreleased structure'''

-	~~The entry~~ 5aow is ~~ON HOLD until Paper~~ Publication	+	==Ternary Crystal Structure of Pyrococcus yayanosii Glyoxylate Hydroxypyruvate Reductase in presence of D-glycerate==
		+	<StructureSection load='5aow' size='340' side='right' caption='[[5aow]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5aow]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AOW FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DGY:(2R)-2,3-DIHYDROXYPROPANOIC+ACID'>DGY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5aov\|5aov]]</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=5aow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aow OCA], [http://pdbe.org/5aow PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aow RCSB], [http://www.ebi.ac.uk/pdbsum/5aow PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Glyoxylate accumulation within cells is highly toxic. In humans, it is associated with hyperoxaluria type 2 (PH2) leading to renal failure. The glyoxylate content within cells is regulated by the NADPH/NADH dependent glyoxylate/hydroxypyruvate reductases (GRHPR). These are highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. Despite the determination of high-resolution X-ray structures, the substrate recognition mode of this class of enzymes remains unclear. We determined the structure at 2.0 A resolution of a thermostable GRHPR from Archaea as a ternary complex in the presence of D-glycerate and NADPH. This shows a binding mode conserved between human and archeal enzymes. We also determined the first structure of GRHPR in presence of glyoxylate at 1.40 A resolution. This revealed the pivotal role of Leu53 and Trp138 in substrate trafficking. These residues act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Taken together, these results allowed us to propose a general model for GRHPR mode of action.

-	~~Authors: Lassalle~~, L., ~~Girard~~, E.	+	New insights into the mechanism of substrates trafficking in Glyoxylate/Hydroxypyruvate reductases.,Lassalle L, Engilberge S, Madern D, Vauclare P, Franzetti B, Girard E Sci Rep. 2016 Feb 11;6:20629. doi: 10.1038/srep20629. PMID:26865263<ref>PMID:26865263</ref>

-	~~Description: Ternary Crystal Structure~~ of ~~Pyrococcus yayanosii Glyoxylate Hydroxypyruvate Reductase in presence~~ of ~~D-glycerate~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
		+	<div class="pdbe-citations 5aow" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Girard, E]]		[[Category: Girard, E]]
	[[Category: Lassalle, L]]		[[Category: Lassalle, L]]
		+	[[Category: Archaea]]
		+	[[Category: D-glycerate]]
		+	[[Category: Glyoxylate hydroxypyruvate reductase]]
		+	[[Category: Oxidoreductase]]

OCA at 09:52, 16 December 2015

2015-12-16T09:52:23Z

←Older revision		Revision as of 09:52, 16 December 2015
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	Description: Ternary Crystal Structure of Pyrococcus yayanosii Glyoxylate Hydroxypyruvate Reductase in presence of D-glycerate		Description: Ternary Crystal Structure of Pyrococcus yayanosii Glyoxylate Hydroxypyruvate Reductase in presence of D-glycerate
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Lassalle, L]]
	[[Category: Girard, E]]		[[Category: Girard, E]]
		+	[[Category: Lassalle, L]]

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

2015-09-30T11:18:10Z

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

←Older revision

Revision as of 11:18, 30 September 2015

OCA: New page: '''Unreleased structure''' The entry 5aow is ON HOLD until Paper Publication Authors: Lassalle, L., Girard, E. Description: Ternary Crystal Structure of Pyrococcus yayanosii Glyoxylate...

2015-09-30T11:18:09Z

New page: '''Unreleased structure''' The entry 5aow is ON HOLD until Paper Publication Authors: Lassalle, L., Girard, E. Description: Ternary Crystal Structure of Pyrococcus yayanosii Glyoxylate...

New page

'''Unreleased structure'''

The entry 5aow is ON HOLD until Paper Publication

Authors: Lassalle, L., Girard, E.

Description: Ternary Crystal Structure of Pyrococcus yayanosii Glyoxylate Hydroxypyruvate Reductase in presence of D-glycerate
[[Category: Unreleased Structures]]
[[Category: Lassalle, L]]
[[Category: Girard, E]]