3b8d: Difference between revisions

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==Fructose 1,6-bisphosphate aldolase from rabbit muscle==
The line below this paragraph, containing "STRUCTURE_3b8d", creates the "Structure Box" on the page.
<StructureSection load='3b8d' size='340' side='right'caption='[[3b8d]], [[Resolution|resolution]] 2.00&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'>[[3b8d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ewg 1ewg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B8D 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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_3b8d| PDB=3b8d |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b8d OCA], [https://pdbe.org/3b8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b8d RCSB], [https://www.ebi.ac.uk/pdbsum/3b8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b8d ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALDOA_RABIT ALDOA_RABIT] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.<ref>PMID:17329259</ref>
== 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/b8/3b8d_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=3b8d ConSurf].
<div style="clear:both"></div>


'''Fructose 1,6-bisphosphate aldolase from rabbit muscle'''
==See Also==
 
*[[Aldolase 3D structures|Aldolase 3D structures]]
 
== References ==
==Overview==
<references/>
The aldolase catalytic cycle consists of a number of proton transfers that interconvert covalent enzyme intermediates. Glu-187 is a conserved amino acid that is located in the mammalian fructose-1,6-bisphosphate aldolase active site. Its central location, within hydrogen bonding distance of three other conserved active site residues: Lys-146, Glu-189, and Schiff base-forming Lys-229, makes it an ideal candidate for mediating proton transfers. Point mutations, Glu-187--&gt; Gln, Ala, which would inhibit proton transfers significantly, compromise activity. Trapping of enzymatic intermediates in Glu-187 mutants defines a proton transfer role for Glu-187 in substrate cleavage and Schiff base formation. Structural data show that loss of Glu-187 negative charge results in hydrogen bond formation between Lys-146 and Lys-229 consistent with a basic pK(a) for Lys-229 in native enzyme and supporting nucleophilic activation of Lys-229 by Glu-187 during Schiff base formation. The crystal structures also substantiate Glu-187 and Glu-189 as present in ionized form in native enzyme, compatible with their role of catalyzing proton exchange with solvent as indicated from solvent isotope effects. The proton exchange mechanism ensures Glu-187 basicity throughout the catalytic cycle requisite for mediating proton transfer and electrostatic stabilization of ketamine intermediates. Glutamate general base catalysis is a recurrent evolutionary feature of Schiff base0forming aldolases.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
3B8D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ewg 1ewg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B8D OCA].
 
==Reference==
A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases., Maurady A, Zdanov A, de Moissac D, Beaudry D, Sygusch J, J Biol Chem. 2002 Mar 15;277(11):9474-83. Epub 2002 Jan 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11779856 11779856]
[[Category: Fructose-bisphosphate aldolase]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Maurady A]]
[[Category: Maurady, A.]]
[[Category: Sygusch J]]
[[Category: Sygusch, J.]]
[[Category: Acetylation]]
[[Category: Aldolase]]
[[Category: Glycolysis]]
[[Category: Phosphorylation]]
[[Category: Schiff base]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 20:30:44 2008''

Latest revision as of 12:27, 21 February 2024

Fructose 1,6-bisphosphate aldolase from rabbit muscleFructose 1,6-bisphosphate aldolase from rabbit muscle

Structural highlights

3b8d is a 4 chain structure with sequence from Oryctolagus cuniculus. This structure supersedes the now removed PDB entry 1ewg. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALDOA_RABIT Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ St-Jean M, Izard T, Sygusch J. A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein. J Biol Chem. 2007 May 11;282(19):14309-15. Epub 2007 Feb 27. PMID:17329259 doi:10.1074/jbc.M611505200

3b8d, resolution 2.00Å

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