3k2q: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (8 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==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=''> | |||
== Structural highlights == | |||
<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='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='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> | |||
</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 == | |||
[[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/k2/3k2q_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=3k2q ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Marinobacter nauticus VT8]] | |||
[[Category: Acton TB]] | |||
[[Category: Baran MC]] | |||
[[Category: Cunningham K]] | |||
[[Category: Hunt JF]] | |||
[[Category: Janjua K]] | |||
[[Category: Lew S]] | |||
[[Category: Liu J]] | |||
[[Category: Montelione GT]] | |||
[[Category: Neely H]] | |||
[[Category: Owens L]] | |||
[[Category: Rost B]] | |||
[[Category: Seetharaman J]] | |||
[[Category: Tong L]] | |||
[[Category: Wang D]] | |||
[[Category: Xiao R]] | |||
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 |
| ||||||||||||||||||