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==Crystal structure of Pyrophosphate-dependent phosphofructokinase from Marinobacter aquaeolei, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET MqR88== | ==Crystal structure of Pyrophosphate-dependent phosphofructokinase from Marinobacter aquaeolei, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET MqR88== | ||
<StructureSection load='3k2q' size='340' side='right' caption='[[3k2q]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='3k2q' size='340' side='right'caption='[[3k2q]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3k2q]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3k2q]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinobacter_nauticus_VT8 Marinobacter nauticus VT8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K2Q FirstGlance]. <br> | ||
</td></tr><tr id=' | </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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3k2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k2q OCA], [https://pdbe.org/3k2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k2q RCSB], [https://www.ebi.ac.uk/pdbsum/3k2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k2q ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A1U3A9_MARN8 A1U3A9_MARN8] Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.[HAMAP-Rule:MF_01978] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k2/3k2q_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k2/3k2q_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/ | </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=3k2q ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Phosphofructokinase | *[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Marinobacter | [[Category: Marinobacter nauticus VT8]] | ||
[[Category: Acton | [[Category: Acton TB]] | ||
[[Category: Baran | [[Category: Baran MC]] | ||
[[Category: Cunningham | [[Category: Cunningham K]] | ||
[[Category: Hunt | [[Category: Hunt JF]] | ||
[[Category: Janjua | [[Category: Janjua K]] | ||
[[Category: Lew | [[Category: Lew S]] | ||
[[Category: Liu | [[Category: Liu J]] | ||
[[Category: Montelione | [[Category: Montelione GT]] | ||
[[Category: Neely H]] | |||
[[Category: Neely | [[Category: Owens L]] | ||
[[Category: Owens | [[Category: Rost B]] | ||
[[Category: Rost | [[Category: Seetharaman J]] | ||
[[Category: Seetharaman | [[Category: Tong L]] | ||
[[Category: Tong | [[Category: Wang D]] | ||
[[Category: Wang | [[Category: Xiao R]] | ||
[[Category: Xiao | |||
Latest revision as of 13:14, 21 February 2024
Crystal structure of Pyrophosphate-dependent phosphofructokinase from Marinobacter aquaeolei, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET MqR88Crystal structure of Pyrophosphate-dependent phosphofructokinase from Marinobacter aquaeolei, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET MqR88
Structural highlights
FunctionA1U3A9_MARN8 Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.[HAMAP-Rule:MF_01978] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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