2qqc: Difference between revisions

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[[Image:2qqc.jpg|left|200px]]


<!--
==E109Q mutant of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii==
The line below this paragraph, containing "STRUCTURE_2qqc", creates the "Structure Box" on the page.
<StructureSection load='2qqc' size='340' side='right'caption='[[2qqc]], [[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'>[[2qqc]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QQC 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>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AG2:AGMATINE'>AG2</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr>
{{STRUCTURE_2qqc|  PDB=2qqc  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qqc OCA], [https://pdbe.org/2qqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qqc RCSB], [https://www.ebi.ac.uk/pdbsum/2qqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qqc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PDAD_METJA PDAD_METJA]
== 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/qq/2qqc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2qqc ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pyruvoyl-dependent arginine decarboxylase (PvlArgDC) catalyzes the first step of the polyamine-biosynthetic pathway in plants and some archaebacteria. The pyruvoyl group of PvlArgDC is generated by an internal autoserinolysis reaction at an absolutely conserved serine residue in the proenzyme, resulting in two polypeptide chains. Based on the native structure of PvlArgDC from Methanococcus jannaschii, the conserved residues Asn47 and Glu109 were proposed to be involved in the decarboxylation and autoprocessing reactions. N47A and E109Q mutant proteins were prepared and the three-dimensional structure of each protein was determined at 2.0 A resolution. The N47A and E109Q mutant proteins showed reduced decarboxylation activity compared with the wild-type PvlArgDC. These residues may also be important for the autoprocessing reaction, which utilizes a mechanism similar to that of the decarboxylation reaction.


'''E109Q mutant of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii'''
Structures of the N47A and E109Q mutant proteins of pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii.,Soriano EV, McCloskey DE, Kinsland C, Pegg AE, Ealick SE Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):377-82. Epub 2008, Mar 19. PMID:18391404<ref>PMID:18391404</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==About this Structure==
</div>
2QQC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QQC OCA].
<div class="pdbe-citations 2qqc" style="background-color:#fffaf0;"></div>
[[Category: Arginine decarboxylase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Protein complex]]
[[Category: Ealick SE]]
[[Category: Ealick, S E.]]
[[Category: Soriano ES]]
[[Category: Soriano, E S.]]
[[Category: Arginine decarboxylase]]
[[Category: Autoprocessing]]
[[Category: Decarboxylation]]
[[Category: Lyase]]
[[Category: Pyruvate]]
[[Category: Pyruvoyl]]
[[Category: Serinolysis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 15:24:46 2008''

Latest revision as of 08:28, 17 October 2024

E109Q mutant of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashiiE109Q mutant of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii

Structural highlights

2qqc is a 12 chain structure with sequence from Methanocaldococcus jannaschii. 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

PDAD_METJA

Evolutionary Conservation

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

Publication Abstract from PubMed

Pyruvoyl-dependent arginine decarboxylase (PvlArgDC) catalyzes the first step of the polyamine-biosynthetic pathway in plants and some archaebacteria. The pyruvoyl group of PvlArgDC is generated by an internal autoserinolysis reaction at an absolutely conserved serine residue in the proenzyme, resulting in two polypeptide chains. Based on the native structure of PvlArgDC from Methanococcus jannaschii, the conserved residues Asn47 and Glu109 were proposed to be involved in the decarboxylation and autoprocessing reactions. N47A and E109Q mutant proteins were prepared and the three-dimensional structure of each protein was determined at 2.0 A resolution. The N47A and E109Q mutant proteins showed reduced decarboxylation activity compared with the wild-type PvlArgDC. These residues may also be important for the autoprocessing reaction, which utilizes a mechanism similar to that of the decarboxylation reaction.

Structures of the N47A and E109Q mutant proteins of pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii.,Soriano EV, McCloskey DE, Kinsland C, Pegg AE, Ealick SE Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):377-82. Epub 2008, Mar 19. PMID:18391404[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Soriano EV, McCloskey DE, Kinsland C, Pegg AE, Ealick SE. Structures of the N47A and E109Q mutant proteins of pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii. Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):377-82. Epub 2008, Mar 19. PMID:18391404 doi:http://dx.doi.org/S0907444908000474

2qqc, resolution 2.00Å

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