1ayl: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(19 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ayl.gif|left|200px]]<br />
<applet load="1ayl" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ayl, resolution 1.8&Aring;" />
'''PHOSPHOENOLPYRUVATE CARBOXYKINASE'''<br />


==Overview==
==PHOSPHOENOLPYRUVATE CARBOXYKINASE==
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.
<StructureSection load='1ayl' size='340' side='right'caption='[[1ayl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>


==About this Structure==
==See Also==
1AYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with OXL, MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Structure known Active Site: ACT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AYL OCA].
*[[Phosphoenolpyruvate carboxykinase 3D structures|Phosphoenolpyruvate carboxykinase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8599762 8599762]
[[Category: Escherichia coli K-12]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Phosphoenolpyruvate carboxykinase (ATP)]]
[[Category: Delbaere LTJ]]
[[Category: Single protein]]
[[Category: Goldie H]]
[[Category: Delbaere, L.T.J.]]
[[Category: Pugazenthi U]]
[[Category: Goldie, H.]]
[[Category: Tari LW]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 15:52:34 2007''
Retrieved from "https://proteopedia.org/1ayl"