1eyi: Difference between revisions

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~~{{Seed}}~~

~~[[Image:1eyi.png|left|200px]]~~

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==FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH MAGNESIUM, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (R-STATE)==

~~The line below this paragraph~~, ~~containing~~ "~~STRUCTURE_1eyi~~", ~~creates the~~ "~~Structure Box~~" on the ~~page~~.

You may ~~change~~ the ~~PDB parameter~~ (~~which sets~~ the ~~PDB file loaded into~~ the ~~applet~~)

== Structural highlights ==

or the ~~SCENE parameter~~ (which ~~sets~~ the ~~initial scene displayed when~~ the ~~page is loaded~~),

<table><tr><td colspan='2'>[[1eyi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EYI FirstGlance]. <br>

~~or leave~~ the ~~SCENE parameter empty~~ for the ~~default display~~.

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.32Å</td></tr>

-->

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

~~{{STRUCTURE_1eyi| PDB=1eyi | SCENE= }}~~

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyi OCA], [https://pdbe.org/1eyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eyi RCSB], [https://www.ebi.ac.uk/pdbsum/1eyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyi ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/F16P1_PIG F16P1_PIG]

== Evolutionary Conservation ==

[[Image:Consurf_key_small.gif|200px|right]]

Check<jmol>

<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ey/1eyi_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/main_output.php?pdb_ID=1eyi ConSurf].

== Publication Abstract from PubMed ==

Crystal structures of metal-product complexes of fructose 1, 6-bisphosphatase (FBPase) reveal competition between AMP and divalent cations. In the presence of AMP, the Zn(2+)-product and Mg(2+)-product complexes have a divalent cation present only at one of three metal binding sites (site 1). The enzyme is in the T-state conformation with a disordered loop of residues 52-72 (loop 52-72). In the absence of AMP, the enzyme crystallizes in the R-state conformation, with loop 52-72 associated with the active site. In structures without AMP, three metal-binding sites are occupied by Zn(2+) and two of three metal sites (sites 1 and 2) by Mg(2+). Evidently, the association of AMP with FBPase disorders loop 52-72, the consequence of which is the release of cations from two of three metal binding sites. In the Mg(2+) complexes (but not the Zn(2+) complexes), the 1-OH group of fructose 6-phosphate (F6P) coordinates to the metal at site 1 and is oriented for a nucleophilic attack on the bound phosphate molecule. A mechanism is presented for the forward reaction, in which Asp74 and Glu98 together generate a hydroxide anion coordinated to the Mg(2+) at site 2, which then displaces F6P. Development of negative charge on the 1-oxygen of F6P is stabilized by its coordination to the Mg(2+) at site 1.

~~===FRUCTOSE-~~1,6-~~BISPHOSPHATASE COMPLEX WITH MAGNESIUM~~, ~~FRUCTOSE-6-PHOSPHATE AND PHOSPHATE~~ (R-~~STATE)===~~

Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes.,Choe JY, Fromm HJ, Honzatko RB Biochemistry. 2000 Jul 25;39(29):8565-74. PMID:10913263<ref>PMID:10913263</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~<!--~~

==See Also==

~~The line below this paragraph, {{ABSTRACT_PUBMED_10913263}}, adds the Publication Abstract to the page~~

*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]

~~(as it appears on PubMed at http://www.pubmed.gov), where 10913263 is the PubMed ID number.~~

== References ==

~~-->~~

~~{{ABSTRACT_PUBMED_10913263}}~~

__TOC__

</StructureSection>

==~~About this Structure~~==

[[Category: Large Structures]]

~~1EYI is a 1 chain structure of sequence from~~ [~~http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from~~ [~~http://oca.weizmann.ac.il/oca~~-~~bin/ocashort?id=1EYI OCA~~].

==~~Reference~~==

<~~ref group="xtra">PMID:10913263<~~/~~ref~~><~~references group="xtra"~~/>

[[Category: ~~Fructose-bisphosphatase~~]]

[[Category: Sus scrofa]]

[[Category: Choe, J.]]

[[Category: Choe J]]

[[Category: Honzatko~~, R B.~~]]

[[Category: Honzatko RB]]

~~[[Category: Allosteric enzyme]]~~

~~[[Category: Bisphosphatase]]~~

~~[[Category: Gluconeogenesis]]~~

~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:11:17 2009''~~

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@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1eyi.png|left|200px]]
-<!--
+==FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH MAGNESIUM, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (R-STATE)==
-The line below this paragraph, containing "STRUCTURE_1eyi", creates the "Structure Box" on the page.
+<StructureSection load='1eyi' size='340' side='right'caption='[[1eyi]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1eyi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EYI FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.32&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-{{STRUCTURE_1eyi|  PDB=1eyi  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyi OCA], [https://pdbe.org/1eyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eyi RCSB], [https://www.ebi.ac.uk/pdbsum/1eyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyi ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/F16P1_PIG F16P1_PIG]
+== 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/ey/1eyi_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/main_output.php?pdb_ID=1eyi ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Crystal structures of metal-product complexes of fructose 1, 6-bisphosphatase (FBPase) reveal competition between AMP and divalent cations. In the presence of AMP, the Zn(2+)-product and Mg(2+)-product complexes have a divalent cation present only at one of three metal binding sites (site 1). The enzyme is in the T-state conformation with a disordered loop of residues 52-72 (loop 52-72). In the absence of AMP, the enzyme crystallizes in the R-state conformation, with loop 52-72 associated with the active site. In structures without AMP, three metal-binding sites are occupied by Zn(2+) and two of three metal sites (sites 1 and 2) by Mg(2+). Evidently, the association of AMP with FBPase disorders loop 52-72, the consequence of which is the release of cations from two of three metal binding sites. In the Mg(2+) complexes (but not the Zn(2+) complexes), the 1-OH group of fructose 6-phosphate (F6P) coordinates to the metal at site 1 and is oriented for a nucleophilic attack on the bound phosphate molecule. A mechanism is presented for the forward reaction, in which Asp74 and Glu98 together generate a hydroxide anion coordinated to the Mg(2+) at site 2, which then displaces F6P. Development of negative charge on the 1-oxygen of F6P is stabilized by its coordination to the Mg(2+) at site 1.
-===FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH MAGNESIUM, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (R-STATE)===
+Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes.,Choe JY, Fromm HJ, Honzatko RB Biochemistry. 2000 Jul 25;39(29):8565-74. PMID:10913263<ref>PMID:10913263</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1eyi" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_10913263}}, adds the Publication Abstract to the page
+*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 10913263 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10913263}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-EYI is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYI OCA].
-==Reference==
-<ref group="xtra">PMID:10913263</ref><references group="xtra"/>
-[[Category: Fructose-bisphosphatase]]
 [[Category: Sus scrofa]]
-[[Category: Choe, J.]]
+[[Category: Choe J]]
-[[Category: Honzatko, R B.]]
+[[Category: Honzatko RB]]
-[[Category: Allosteric enzyme]]
-[[Category: Bisphosphatase]]
-[[Category: Gluconeogenesis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:11:17 2009''