3qpv - Revision history

OCA at 10:49, 21 February 2024

OCA — Wed, 21 Feb 2024 10:49:04 GMT

←Older revision		Revision as of 10:49, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='3qpv' size='340' side='right'caption='[[3qpv]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3qpv' size='340' side='right'caption='[[3qpv]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3qpv]] is a 1 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=3QPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3qpv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene>, <scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene>~~</td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.5Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qpu\|3qpu]], [[3qpw\|3qpw]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene>, <scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PFKFB3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=3qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpv OCA], [https://pdbe.org/3qpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpv RCSB], [https://www.ebi.ac.uk/pdbsum/3qpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpv 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=3qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpv OCA], [https://pdbe.org/3qpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpv RCSB], [https://www.ebi.ac.uk/pdbsum/3qpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/F263_HUMAN F263_HUMAN]] Synthesis and degradation of fructose 2,6-bisphosphate.	+	[https://www.uniprot.org/uniprot/F263_HUMAN F263_HUMAN] Synthesis and degradation of fructose 2,6-bisphosphate.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The molecular basis of Fructose-2,6-bisphosphatase (F-2,6-P(2) ase) of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB) was investigated using the crystal structures of the human inducible form (PFKFB3) in a phospho-enzyme intermediate state (PFKFB3-PF-6-P), in a transition state-analogous complex (PFKFB3AlF4), and in a complex with pyrophosphate (PFKFB3PP(i) ) at resolutions of 2.45A, 2.2A, and 2.3A, respectively. Trapping the PFKFB3-PF-6-P intermediate was achieved by flash cooling the crystal during the reaction, and the PFKFB3AlF4 and PFKFB3PP(i) complexes were obtained by soaking. The PFKFB3AlF(4) and PFKFB3PP(i) complexes resulted in removing F-6-P from the catalytic pocket. With these structures, the structures of the Michaelis complex and the transition state were extrapolated. For both the PFKFB3-P formation and break down, the phosphoryl donor and the acceptor are located within approximately 5.1A, and the pivotal point 2-P is on the same line, suggesting an "in-line" transfer with a direct inversion of phosphate configuration. The geometry suggests that NE2 of His253 undergoes a nucleophilic attack to form a covalent N-P bond, breaking the 2O-P bond in the substrate. The resulting high reactivity of the leaving group, 2O of F-6-P, is neutralized by a proton donated by Glu322. Negative charges on the equatorial oxygens of the transient bipyramidal phosphorane formed during the transfer are stabilized by Arg252, His387, and Asn259. The C-terminal domain (residues 440-446) was rearranged in PFKFB3*PP(i) , implying that this domain plays a critical role in binding of substrate to and release of product from the F-2,6-P(2) ase catalytic pocket. These findings provide a new insight into the understanding of the phosphoryl transfer reaction. Proteins 2011. (c) 2011 Wiley-Liss, Inc.	+
-		+
-	Molecular basis of the Fructose-2,6-bisphosphatase reaction of PFKFB3: Transition state and the C-terminal function.,Cavalier MC, Kim SG, Neau D, Lee YH Proteins. 2011 Dec 21. doi: 10.1002/prot.24015. PMID:22275052<ref>PMID:22275052</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3qpv" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Cavalier~~, M C~~]]	+	[[Category: Cavalier MC]]
-	[[Category: Kim~~, S G~~]]	+	[[Category: Kim SG]]
-	[[Category: Lee~~, Y H~~]]	+	[[Category: Lee YH]]
-	[[Category: Neau, D]]	+	[[Category: Neau D]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Kinase/bisphosphatase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 06:18, 8 June 2022

OCA — Wed, 08 Jun 2022 06:18:51 GMT

←Older revision		Revision as of 06:18, 8 June 2022
Line 1:		Line 1:

	==PFKFB3 trapped in a phospho-enzyme intermediate state==		==PFKFB3 trapped in a phospho-enzyme intermediate state==
-	<StructureSection load='3qpv' size='340' side='right' caption='[[3qpv]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='3qpv' size='340' side='right'caption='[[3qpv]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3qpv]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3QPV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3qpv]] is a 1 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=3QPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene>, <scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene>, <scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3qpu\|3qpu]], [[3qpw\|3qpw]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qpu\|3qpu]], [[3qpw\|3qpw]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PFKFB3 ([~~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">PFKFB3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpv OCA], [~~http~~://pdbe.org/3qpv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3qpv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3qpv PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpv 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=3qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpv OCA], [https://pdbe.org/3qpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpv RCSB], [https://www.ebi.ac.uk/pdbsum/3qpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/F263_HUMAN F263_HUMAN]] Synthesis and degradation of fructose 2,6-bisphosphate.	+	[[https://www.uniprot.org/uniprot/F263_HUMAN F263_HUMAN]] Synthesis and degradation of fructose 2,6-bisphosphate.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Cavalier, M C]]		[[Category: Cavalier, M C]]
	[[Category: Kim, S G]]		[[Category: Kim, S G]]

OCA at 07:42, 5 August 2016

OCA — Fri, 05 Aug 2016 07:42:56 GMT

←Older revision		Revision as of 07:42, 5 August 2016
Line 1:		Line 1:
		+
	==PFKFB3 trapped in a phospho-enzyme intermediate state==		==PFKFB3 trapped in a phospho-enzyme intermediate state==
	<StructureSection load='3qpv' size='340' side='right' caption='[[3qpv]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3qpv' size='340' side='right' caption='[[3qpv]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3qpv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QPV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3qpv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QPV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene>, <scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene>, <scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3qpu\|3qpu]], [[3qpw\|3qpw]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3qpu\|3qpu]], [[3qpw\|3qpw]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PFKFB3 ([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">PFKFB3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qpv RCSB], [http://www.ebi.ac.uk/pdbsum/3qpv 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=3qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpv OCA], [http://pdbe.org/3qpv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qpv RCSB], [http://www.ebi.ac.uk/pdbsum/3qpv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 3qpv" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Cavalier, M C]]		[[Category: Cavalier, M C]]
	[[Category: Kim, S G]]		[[Category: Kim, S G]]

OCA at 00:23, 25 December 2014

OCA — Thu, 25 Dec 2014 00:23:47 GMT

←Older revision		Revision as of 00:23, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3qpv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QPV FirstGlance]. <br>		<table><tr><td colspan='2'>[[3qpv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QPV FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene>, <scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene>, <scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3qpu\|3qpu]], [[3qpw\|3qpw]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3qpu\|3qpu]], [[3qpw\|3qpw]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PFKFB3 ([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">PFKFB3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qpv RCSB], [http://www.ebi.ac.uk/pdbsum/3qpv 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=3qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qpv RCSB], [http://www.ebi.ac.uk/pdbsum/3qpv PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/F263_HUMAN F263_HUMAN]] Synthesis and degradation of fructose 2,6-bisphosphate.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 16:
	Molecular basis of the Fructose-2,6-bisphosphatase reaction of PFKFB3: Transition state and the C-terminal function.,Cavalier MC, Kim SG, Neau D, Lee YH Proteins. 2011 Dec 21. doi: 10.1002/prot.24015. PMID:22275052<ref>PMID:22275052</ref>		Molecular basis of the Fructose-2,6-bisphosphatase reaction of PFKFB3: Transition state and the C-terminal function.,Cavalier MC, Kim SG, Neau D, Lee YH Proteins. 2011 Dec 21. doi: 10.1002/prot.24015. PMID:22275052<ref>PMID:22275052</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 21:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Cavalier, M C.]]	+	[[Category: Cavalier, M C]]
-	[[Category: Kim, S G.]]	+	[[Category: Kim, S G]]
-	[[Category: Lee, Y H.]]	+	[[Category: Lee, Y H]]
-	[[Category: Neau, D.]]	+	[[Category: Neau, D]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Kinase/bisphosphatase]]		[[Category: Kinase/bisphosphatase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 05:31, 4 June 2014

OCA — Wed, 04 Jun 2014 05:31:42 GMT

←Older revision		Revision as of 05:31, 4 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3qpv.~~png~~\|~~left~~\|~~200px~~]]	+	==PFKFB3 trapped in a phospho-enzyme intermediate state==
		+	<StructureSection load='3qpv' size='340' side='right' caption='[[3qpv]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3qpv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QPV FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene>, <scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3qpu\|3qpu]], [[3qpw\|3qpw]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PFKFB3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qpv RCSB], [http://www.ebi.ac.uk/pdbsum/3qpv PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The molecular basis of Fructose-2,6-bisphosphatase (F-2,6-P(2) ase) of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB) was investigated using the crystal structures of the human inducible form (PFKFB3) in a phospho-enzyme intermediate state (PFKFB3-PF-6-P), in a transition state-analogous complex (PFKFB3AlF4), and in a complex with pyrophosphate (PFKFB3PP(i) ) at resolutions of 2.45A, 2.2A, and 2.3A, respectively. Trapping the PFKFB3-PF-6-P intermediate was achieved by flash cooling the crystal during the reaction, and the PFKFB3AlF4 and PFKFB3PP(i) complexes were obtained by soaking. The PFKFB3AlF(4) and PFKFB3PP(i) complexes resulted in removing F-6-P from the catalytic pocket. With these structures, the structures of the Michaelis complex and the transition state were extrapolated. For both the PFKFB3-P formation and break down, the phosphoryl donor and the acceptor are located within approximately 5.1A, and the pivotal point 2-P is on the same line, suggesting an "in-line" transfer with a direct inversion of phosphate configuration. The geometry suggests that NE2 of His253 undergoes a nucleophilic attack to form a covalent N-P bond, breaking the 2O-P bond in the substrate. The resulting high reactivity of the leaving group, 2O of F-6-P, is neutralized by a proton donated by Glu322. Negative charges on the equatorial oxygens of the transient bipyramidal phosphorane formed during the transfer are stabilized by Arg252, His387, and Asn259. The C-terminal domain (residues 440-446) was rearranged in PFKFB3*PP(i) , implying that this domain plays a critical role in binding of substrate to and release of product from the F-2,6-P(2) ase catalytic pocket. These findings provide a new insight into the understanding of the phosphoryl transfer reaction. Proteins 2011. (c) 2011 Wiley-Liss, Inc.

-	<!--	+	Molecular basis of the Fructose-2,6-bisphosphatase reaction of PFKFB3: Transition state and the C-terminal function.,Cavalier MC, Kim SG, Neau D, Lee YH Proteins. 2011 Dec 21. doi: 10.1002/prot.24015. PMID:22275052<ref>PMID:22275052</ref>
-	~~The line below this paragraph, containing "STRUCTURE_3qpv", 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_3qpv\| PDB=3qpv \| SCENE= }}~~	+

-	~~===PFKFB3 trapped in~~ a ~~phospho-enzyme intermediate state===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_22275052}}, adds~~ the ~~Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 22275052 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_22275052}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3qpv]] is a 1 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPV OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:022275052<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Cavalier, M C.]]		[[Category: Cavalier, M C.]]

OCA at 06:41, 21 March 2012

OCA — Wed, 21 Mar 2012 06:41:38 GMT

←Older revision		Revision as of 06:41, 21 March 2012
Line 1:		Line 1:
-	[[Image:3qpv.~~jpg~~\|left\|200px]]	+	[[Image:3qpv.png\|left\|200px]]

	<!--		<!--

OCA at 06:29, 8 February 2012

OCA — Wed, 08 Feb 2012 06:29:56 GMT

←Older revision		Revision as of 06:29, 8 February 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3qpv.jpg\|left\|200px]]

-	The ~~entry 3qpv~~ is ~~ON HOLD~~ ~~until 00 0001~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3qpv", 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_3qpv\| PDB=3qpv \| SCENE= }}

-	~~Authors: Cavalier, M.C., Kim, S.G., Neau, D., Lee, Y.H.~~	+	===PFKFB3 trapped in a phospho-enzyme intermediate state===

-	~~Description~~: ~~PFKFB3 trapped in~~ a ~~phospho~~-~~enzyme intermediate state~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22275052}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22275052 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22275052}}
		+
		+	==About this Structure==
		+	[[3qpv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPV OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022275052</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Cavalier, M C.]]
		+	[[Category: Kim, S G.]]
		+	[[Category: Lee, Y H.]]
		+	[[Category: Neau, D.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Kinase/bisphosphatase]]
		+	[[Category: Transferase]]

OCA at 05:53, 25 January 2012

OCA — Wed, 25 Jan 2012 05:53:15 GMT

←Older revision		Revision as of 05:53, 25 January 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3qpv is ON HOLD until ~~Paper Publication~~	+	The entry 3qpv is ON HOLD until 00 0001

	Authors: Cavalier, M.C., Kim, S.G., Neau, D., Lee, Y.H.		Authors: Cavalier, M.C., Kim, S.G., Neau, D., Lee, Y.H.

	Description: PFKFB3 trapped in a phospho-enzyme intermediate state		Description: PFKFB3 trapped in a phospho-enzyme intermediate state

OCA at 08:03, 16 March 2011

OCA — Wed, 16 Mar 2011 08:03:06 GMT

←Older revision		Revision as of 08:03, 16 March 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Cavalier, M.C., Kim, S.G., Neau, D., Lee, Y.H.		Authors: Cavalier, M.C., Kim, S.G., Neau, D., Lee, Y.H.

	Description: PFKFB3 trapped in a phospho-enzyme intermediate state		Description: PFKFB3 trapped in a phospho-enzyme intermediate state

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

OCA — Wed, 23 Feb 2011 09:40:20 GMT

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

←Older revision

Revision as of 09:40, 23 February 2011