1rdz: Difference between revisions

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[[Image:1rdz.jpg|left|200px]]


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==T-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI==
The line below this paragraph, containing "STRUCTURE_1rdz", creates the "Structure Box" on the page.
<StructureSection load='1rdz' size='340' side='right'caption='[[1rdz]], [[Resolution|resolution]] 2.05&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'>[[1rdz]] is a 2 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=1RDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RDZ 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]] 2.05&#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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene></td></tr>
{{STRUCTURE_1rdz| PDB=1rdz |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rdz OCA], [https://pdbe.org/1rdz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rdz RCSB], [https://www.ebi.ac.uk/pdbsum/1rdz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rdz 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/rd/1rdz_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=1rdz ConSurf].
<div style="clear:both"></div>


'''T-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI'''
==See Also==
 
*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The active site of pig kidney fructose-1,6-bisphosphatase (EC 3.1.3.11) is shared between subunits, Arg-243 of one chain interacting with fructose-1,6-bisphosphate or fructose-2,6-bisphosphate in the active site of an adjacent chain. In this study, we present the X-ray structures of the mutant version of the enzyme with Arg-243 replaced by alanine, crystallized in both T and R allosteric states. Kinetic characteristics of the altered enzyme showed the magnesium binding and inhibition by AMP differed slightly; affinity for the substrate fructose-1,6-bisphosphate was reduced 10-fold and affinity for the inhibitor fructose-2,6-bisphosphate was reduced 1,000-fold (Giroux E, Williams MK, Kantrowitz ER, 1994, J Biol Chem 269:31404-31409). The X-ray structures show no major changes in the organization of the active site compared with wild-type enzyme, and the structures confirm predictions of molecular dynamics simulations involving Lys-269 and Lys-274. Comparison of two independent models of the T form structures have revealed small but significant changes in the conformation of the bound AMP molecules and small reorganization of the active site correlated with the presence of the inhibitor. The differences in kinetic properties of the mutant enzyme indicate the key importance of Arg-243 in the function of fructose-1,6-bisphosphatase. Calculations using the X-ray structures of the Arg-243--&gt;Ala enzyme suggest that the role of Arg-243 in the wild-type enzyme is predominantly electrostatic in nature.
[[Category: Large Structures]]
 
==About this Structure==
1RDZ is a [[Single protein]] 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=1RDZ OCA].
 
==Reference==
Crystal structures of the active site mutant (Arg-243--&gt;Ala) in the T and R allosteric states of pig kidney fructose-1,6-bisphosphatase expressed in Escherichia coli., Stec B, Abraham R, Giroux E, Kantrowitz ER, Protein Sci. 1996 Aug;5(8):1541-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8844845 8844845]
[[Category: Fructose-bisphosphatase]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Abraham, R.]]
[[Category: Abraham R]]
[[Category: Giroux, E.]]
[[Category: Giroux E]]
[[Category: Kantrowitz, E R.]]
[[Category: Kantrowitz ER]]
[[Category: Stec, B.]]
[[Category: Stec B]]
[[Category: Hydrolase r243a mutant in the t-state]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:22:47 2008''

Latest revision as of 11:22, 14 February 2024

T-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLIT-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI

Structural highlights

1rdz is a 2 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.05Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

F16P1_PIG

Evolutionary Conservation

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

See Also

1rdz, resolution 2.05Å

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