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[[Image:1ayl.gif|left|200px]]


{{Structure
==PHOSPHOENOLPYRUVATE CARBOXYKINASE==
|PDB= 1ayl |SIZE=350|CAPTION= <scene name='initialview01'>1ayl</scene>, resolution 1.8&Aring;
<StructureSection load='1ayl' size='340' side='right'caption='[[1ayl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE= <scene name='pdbsite=ACT:Putative+Active+Site+Residues'>ACT</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>
<table><tr><td colspan='2'>[[1ayl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AYL FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(ATP) Phosphoenolpyruvate carboxykinase (ATP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.49 4.1.1.49]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</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=1ayl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayl OCA], [https://pdbe.org/1ayl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ayl RCSB], [https://www.ebi.ac.uk/pdbsum/1ayl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ayl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PCKA_ECOLI PCKA_ECOLI]
== 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/ay/1ayl_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=1ayl ConSurf].
<div style="clear:both"></div>


'''PHOSPHOENOLPYRUVATE CARBOXYKINASE'''
==See Also==
 
*[[Phosphoenolpyruvate carboxykinase 3D structures|Phosphoenolpyruvate carboxykinase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
We report the 1.8 A crystal structure of adenosine triphosphate (ATP)-magnesium-oxalate bound phosphoenolpyruvate carboxykinase (PCK) from Escherichia coli. ATP binding induces a 20 degree hinge-like rotation of the N- and C-terminal domains which closes the active-site cleft. PCK possesses a novel nucleotide-binding fold, particularly in the adenine-binding region, where the formation of a cis backbone torsion angle in a loop glycine residue promotes intimate contacts between the adenine-binding loop and adenine, while stabilizing a syn conformation of the base. This complex represents a reaction intermediate analogue along the pathway of the conversion of oxaloacetate to phosphoenolpyruvate, and provides insight into the mechanistic details of the chemical reaction catalysed by this enzyme.
[[Category: Escherichia coli K-12]]
 
[[Category: Large Structures]]
==About this Structure==
[[Category: Delbaere LTJ]]
1AYL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYL OCA].
[[Category: Goldie H]]
 
[[Category: Pugazenthi U]]
==Reference==
[[Category: Tari LW]]
Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase., Tari LW, Matte A, Pugazhenthi U, Goldie H, Delbaere LT, Nat Struct Biol. 1996 Apr;3(4):355-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8599762 8599762]
[[Category: Escherichia coli]]
[[Category: Phosphoenolpyruvate carboxykinase (ATP)]]
[[Category: Single protein]]
[[Category: Delbaere, L T.J.]]
[[Category: Goldie, H.]]
[[Category: Pugazenthi, U.]]
[[Category: Tari, L W.]]
[[Category: ATP]]
[[Category: MG]]
[[Category: OXL]]
[[Category: kinase (transphosphorylating)]]
[[Category: nucleotide-triphosphate hydrolase]]
[[Category: p-loop]]
[[Category: protein-atp complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:03:56 2008''

Latest revision as of 06:34, 7 February 2024

PHOSPHOENOLPYRUVATE CARBOXYKINASE

1ayl, resolution 1.80Å

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