2bhl - Revision history

OCA at 13:38, 13 December 2023

OCA — Wed, 13 Dec 2023 13:38:17 GMT

←Older revision		Revision as of 13:38, 13 December 2023
Line 1:		Line 1:

	==X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE==		==X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE==
-	<StructureSection load='2bhl' size='340' side='right'caption='[[2bhl]]' scene=''>	+	<StructureSection load='2bhl' size='340' side='right'caption='[[2bhl]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BHL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2bhl]] is a 2 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=2BHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BHL FirstGlance]. <br>
-	</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=2bhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhl OCA], [https://pdbe.org/2bhl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bhl RCSB], [https://www.ebi.ac.uk/pdbsum/2bhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bhl ProSAT]</span></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]] 2.9Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=2bhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhl OCA], [https://pdbe.org/2bhl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bhl RCSB], [https://www.ebi.ac.uk/pdbsum/2bhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bhl ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[https://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN] Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) [MIM:[https://omim.org/entry/305900 305900]. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.<ref>PMID:1611091</ref>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN] Produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 16:		Line 22:
	</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=2bhl 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=2bhl ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human glucose-6-phosphate dehydrogenase (G6PD) is NADP(+)-dependent and catalyses the first and rate-limiting step of the pentose phosphate shunt. Binary complexes of the human deletion mutant, DeltaG6PD, with glucose-6-phosphate and NADP(+) have been crystallized and their structures solved to 2.9 and 2.5 A, respectively. The structures are compared with the previously determined structure of the Canton variant of human G6PD (G6PD(Canton)) in which NADP(+) is bound at the structural site. Substrate binding in DeltaG6PD is shown to be very similar to that described previously in Leuconostoc mesenteroides G6PD. NADP(+) binding at the coenzyme site is seen to be comparable to NADP(+) binding in L. mesenteroides G6PD, although some differences arise as a result of sequence changes. The tetramer interface varies slightly among the human G6PD complexes, suggesting flexibility in the predominantly hydrophilic dimer-dimer interactions. In both complexes, Pro172 of the conserved peptide EKPxG is in the cis conformation; it is seen to be crucial for close approach of the substrate and coenzyme during the enzymatic reaction. Structural NADP(+) binds in a very similar way in the DeltaG6PD-NADP(+) complex and in G6PD(Canton), while in the substrate complex the structural NADP(+) has low occupancy and the C-terminal tail at the structural NADP(+) site is disordered. The implications of possible interaction between the structural NADP(+) and G6P are considered.
		+
		+	Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase.,Kotaka M, Gover S, Vandeputte-Rutten L, Au SW, Lam VM, Adams MJ Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):495-504. Epub 2005, Apr 20. PMID:15858258<ref>PMID:15858258</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 2bhl" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Glucose 6-phosphate dehydrogenase\|Glucose 6-phosphate dehydrogenase]]		*[[Glucose 6-phosphate dehydrogenase\|Glucose 6-phosphate dehydrogenase]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Adams MJ]]		[[Category: Adams MJ]]

OCA at 15:25, 3 March 2021

OCA — Wed, 03 Mar 2021 15:25:40 GMT

←Older revision		Revision as of 15:25, 3 March 2021
Line 1:		Line 1:

	==X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE==		==X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE==
-	<StructureSection load='2bhl' size='340' side='right'caption='[[2bhl]]~~, [[Resolution\|resolution]] 2.90Å~~' scene=''>	+	<StructureSection load='2bhl' size='340' side='right'caption='[[2bhl]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[2bhl]] is a 2 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=2BHL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2BHL FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BHL FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>	+	</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=2bhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhl OCA], [https://pdbe.org/2bhl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bhl RCSB], [https://www.ebi.ac.uk/pdbsum/2bhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bhl ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]], [[2bh9\|2bh9]]</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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=2bhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhl OCA], [~~http~~://pdbe.org/2bhl PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2bhl RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2bhl PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2bhl ProSAT]</span></td></tr>	+
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 19:		Line 16:
	</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=2bhl 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=2bhl ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Human glucose-6-phosphate dehydrogenase (G6PD) is NADP(+)-dependent and catalyses the first and rate-limiting step of the pentose phosphate shunt. Binary complexes of the human deletion mutant, DeltaG6PD, with glucose-6-phosphate and NADP(+) have been crystallized and their structures solved to 2.9 and 2.5 A, respectively. The structures are compared with the previously determined structure of the Canton variant of human G6PD (G6PD(Canton)) in which NADP(+) is bound at the structural site. Substrate binding in DeltaG6PD is shown to be very similar to that described previously in Leuconostoc mesenteroides G6PD. NADP(+) binding at the coenzyme site is seen to be comparable to NADP(+) binding in L. mesenteroides G6PD, although some differences arise as a result of sequence changes. The tetramer interface varies slightly among the human G6PD complexes, suggesting flexibility in the predominantly hydrophilic dimer-dimer interactions. In both complexes, Pro172 of the conserved peptide EKPxG is in the cis conformation; it is seen to be crucial for close approach of the substrate and coenzyme during the enzymatic reaction. Structural NADP(+) binds in a very similar way in the DeltaG6PD-NADP(+) complex and in G6PD(Canton), while in the substrate complex the structural NADP(+) has low occupancy and the C-terminal tail at the structural NADP(+) site is disordered. The implications of possible interaction between the structural NADP(+) and G6P are considered.
-
-	Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase.,Kotaka M, Gover S, Vandeputte-Rutten L, Au SW, Lam VM, Adams MJ Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):495-504. Epub 2005, Apr 20. PMID:15858258<ref>PMID:15858258</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2bhl" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Glucose 6-phosphate dehydrogenase\|Glucose 6-phosphate dehydrogenase]]		*[[Glucose 6-phosphate dehydrogenase\|Glucose 6-phosphate dehydrogenase]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Glucose-6-phosphate dehydrogenase]]
-	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Adams~~, M J~~]]	+	[[Category: Adams MJ]]
-	[[Category: Gover, S]]	+	[[Category: Gover S]]
-	[[Category: Kotaka, M]]	+	[[Category: Kotaka M]]
-	[[Category: Lam~~, V M.S]]~~	+	[[Category: Lam VMS]]
-	~~[[Category: Glucose metabolism]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 07:09, 23 May 2019

OCA — Thu, 23 May 2019 07:09:59 GMT

←Older revision		Revision as of 07:09, 23 May 2019
Line 1:		Line 1:

	==X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE==		==X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE==
-	<StructureSection load='2bhl' size='340' side='right' caption='[[2bhl]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<StructureSection load='2bhl' size='340' side='right'caption='[[2bhl]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bhl]] is a 2 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=2BHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BHL FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bhl]] is a 2 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=2BHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BHL FirstGlance]. <br>
Line 37:		Line 37:
	[[Category: Glucose-6-phosphate dehydrogenase]]		[[Category: Glucose-6-phosphate dehydrogenase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Adams, M J]]		[[Category: Adams, M J]]
	[[Category: Gover, S]]		[[Category: Gover, S]]

OCA at 06:17, 16 May 2018

OCA — Wed, 16 May 2018 06:17:16 GMT

←Older revision		Revision as of 06:17, 16 May 2018
Line 1:		Line 1:
		+
	==X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE==		==X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE==
	<StructureSection load='2bhl' size='340' side='right' caption='[[2bhl]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='2bhl' size='340' side='right' caption='[[2bhl]], [[Resolution\|resolution]] 2.90Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]], [[2bh9\|2bh9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]], [[2bh9\|2bh9]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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=2bhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhl OCA], [http://pdbe.org/2bhl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bhl RCSB], [http://www.ebi.ac.uk/pdbsum/2bhl 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=2bhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhl OCA], [http://pdbe.org/2bhl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bhl RCSB], [http://www.ebi.ac.uk/pdbsum/2bhl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bhl ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/2bhl_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/2bhl_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>
	</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=2bhl ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 2bhl" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2bhl" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glucose 6-phosphate dehydrogenase\|Glucose 6-phosphate dehydrogenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:17, 11 September 2015

OCA — Fri, 11 Sep 2015 08:17:38 GMT

←Older revision		Revision as of 08:17, 11 September 2015
Line 6:		Line 6:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]], [[2bh9\|2bh9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]], [[2bh9\|2bh9]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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=2bhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bhl RCSB], [http://www.ebi.ac.uk/pdbsum/2bhl 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=2bhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhl OCA], [http://pdbe.org/2bhl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bhl RCSB], [http://www.ebi.ac.uk/pdbsum/2bhl PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 26:		Line 26:
	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 2bhl" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:02, 8 January 2015

OCA — Thu, 08 Jan 2015 10:02:22 GMT

←Older revision		Revision as of 10:02, 8 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bhl]] is a 2 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=2BHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BHL FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bhl]] is a 2 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=2BHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BHL FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]], [[2bh9\|2bh9]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]], [[2bh9\|2bh9]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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=2bhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bhl RCSB], [http://www.ebi.ac.uk/pdbsum/2bhl 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=2bhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bhl RCSB], [http://www.ebi.ac.uk/pdbsum/2bhl PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:
	[[Category: Glucose-6-phosphate dehydrogenase]]		[[Category: Glucose-6-phosphate dehydrogenase]]
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Adams, M J.]]	+	[[Category: Adams, M J]]
-	[[Category: Gover, S.]]	+	[[Category: Gover, S]]
-	[[Category: Kotaka, M.]]	+	[[Category: Kotaka, M]]
-	[[Category: Lam, V M.S.]]	+	[[Category: Lam, V M.S]]
	[[Category: Glucose metabolism]]		[[Category: Glucose metabolism]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 05:16, 3 October 2014

OCA — Fri, 03 Oct 2014 05:16:31 GMT

←Older revision		Revision as of 05:16, 3 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2bhl\| PDB=2bhl \| SCENE= }}~~	+	==X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE==
-	===X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE===	+	<StructureSection load='2bhl' size='340' side='right' caption='[[2bhl]], [[Resolution\|resolution]] 2.90Å' scene=''>
-	~~{{ABSTRACT_PUBMED_15858258}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2bhl]] is a 2 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=2BHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BHL FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]], [[2bh9\|2bh9]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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=2bhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bhl RCSB], [http://www.ebi.ac.uk/pdbsum/2bhl PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/2bhl_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 ==
		+	Human glucose-6-phosphate dehydrogenase (G6PD) is NADP(+)-dependent and catalyses the first and rate-limiting step of the pentose phosphate shunt. Binary complexes of the human deletion mutant, DeltaG6PD, with glucose-6-phosphate and NADP(+) have been crystallized and their structures solved to 2.9 and 2.5 A, respectively. The structures are compared with the previously determined structure of the Canton variant of human G6PD (G6PD(Canton)) in which NADP(+) is bound at the structural site. Substrate binding in DeltaG6PD is shown to be very similar to that described previously in Leuconostoc mesenteroides G6PD. NADP(+) binding at the coenzyme site is seen to be comparable to NADP(+) binding in L. mesenteroides G6PD, although some differences arise as a result of sequence changes. The tetramer interface varies slightly among the human G6PD complexes, suggesting flexibility in the predominantly hydrophilic dimer-dimer interactions. In both complexes, Pro172 of the conserved peptide EKPxG is in the cis conformation; it is seen to be crucial for close approach of the substrate and coenzyme during the enzymatic reaction. Structural NADP(+) binds in a very similar way in the DeltaG6PD-NADP(+) complex and in G6PD(Canton), while in the substrate complex the structural NADP(+) has low occupancy and the C-terminal tail at the structural NADP(+) site is disordered. The implications of possible interaction between the structural NADP(+) and G6P are considered.

-	~~==About this Structure==~~	+	Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase.,Kotaka M, Gover S, Vandeputte-Rutten L, Au SW, Lam VM, Adams MJ Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):495-504. Epub 2005, Apr 20. PMID:15858258<ref>PMID:15858258</ref>
-	~~[[2bhl]] is a 2 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=2BHL OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:015858258</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Glucose-6-phosphate dehydrogenase]]		[[Category: Glucose-6-phosphate dehydrogenase]]
	[[Category: Human]]		[[Category: Human]]

OCA at 08:15, 5 February 2014

OCA — Wed, 05 Feb 2014 08:15:36 GMT

←Older revision		Revision as of 08:15, 5 February 2014
Line 4:		Line 4:

	==About this Structure==		==About this Structure==
-	[[2bhl]] is a 2 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=2BHL OCA].	+	[[2bhl]] is a 2 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=2BHL OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:015858258~~</ref><ref group="xtra">PMID:010745013~~</ref><references group="xtra"/><references/>	+	<ref group="xtra">PMID:015858258</ref><references group="xtra"/><references/>
	[[Category: Glucose-6-phosphate dehydrogenase]]		[[Category: Glucose-6-phosphate dehydrogenase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Adams, M J.]]		[[Category: Adams, M J.]]
	[[Category: Gover, S.]]		[[Category: Gover, S.]]
	[[Category: Kotaka, M.]]		[[Category: Kotaka, M.]]
	[[Category: Lam, V M.S.]]		[[Category: Lam, V M.S.]]
		+	[[Category: Glucose metabolism]]
		+	[[Category: Oxidoreductase]]

OCA at 04:22, 25 March 2013

OCA — Mon, 25 Mar 2013 04:22:07 GMT

←Older revision		Revision as of 04:22, 25 March 2013
Line 1:		Line 1:
-	[[Image:2bhl.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_2bhl", 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_2bhl\| PDB=2bhl \| SCENE= }}		{{STRUCTURE_2bhl\| PDB=2bhl \| SCENE= }}
-
	===X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE===		===X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE===
-
-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15858258}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15858258 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_15858258}}		{{ABSTRACT_PUBMED_15858258}}

Line 22:		Line 7:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15858258~~</ref><ref group="xtra">PMID:~~10745013~~</ref><~~ref~~ group="xtra"~~>PMID:10089300<~~/~~ref~~><references ~~group="xtra"~~/>	+	<ref group="xtra">PMID:015858258</ref><ref group="xtra">PMID:010745013</ref><references group="xtra"/><references/>
	[[Category: Glucose-6-phosphate dehydrogenase]]		[[Category: Glucose-6-phosphate dehydrogenase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA: Protected "2bhl" [edit=sysop:move=sysop]

OCA — Mon, 14 Mar 2011 19:48:30 GMT

Protected "2bhl" [edit=sysop:move=sysop]

←Older revision

Revision as of 19:48, 14 March 2011