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


{{Structure
==Glycine 24 to Serine mutation of aspartate decarboxylase==
|PDB= 1pqf |SIZE=350|CAPTION= <scene name='initialview01'>1pqf</scene>, resolution 2.00&Aring;
<StructureSection load='1pqf' size='340' side='right'caption='[[1pqf]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
<table><tr><td colspan='2'>[[1pqf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PQF FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_1-decarboxylase Aspartate 1-decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.11 4.1.1.11]  
</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>
|GENE= PAND ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1pqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pqf OCA], [https://pdbe.org/1pqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pqf RCSB], [https://www.ebi.ac.uk/pdbsum/1pqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pqf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PAND_ECOLI PAND_ECOLI] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.<ref>PMID:6767707</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/pq/1pqf_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=1pqf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aspartate decarboxylase, which is translated as a pro-protein, undergoes intramolecular self-cleavage at Gly24-Ser25. We have determined the crystal structures of an unprocessed native precursor, in addition to Ala24 insertion, Ala26 insertion and Gly24--&gt;Ser, His11--&gt;Ala, Ser25--&gt;Ala, Ser25--&gt;Cys and Ser25--&gt;Thr mutants. Comparative analyses of the cleavage site reveal specific conformational constraints that govern self-processing and demonstrate that considerable rearrangement must occur. We suggest that Thr57 Ogamma and a water molecule form an 'oxyanion hole' that likely stabilizes the proposed oxyoxazolidine intermediate. Thr57 and this water molecule are probable catalytic residues able to support acid-base catalysis. The conformational freedom in the loop preceding the cleavage site appears to play a determining role in the reaction. The molecular mechanism of self-processing, presented here, emphasizes the importance of stabilization of the oxyoxazolidine intermediate. Comparison of the structural features shows significant similarity to those in other self-processing systems, and suggests that models of the cleavage site of such enzymes based on Ser--&gt;Ala or Ser--&gt;Thr mutants alone may lead to erroneous interpretations of the mechanism.


'''Glycine 24 to Serine mutation of aspartate decarboxylase'''
Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase.,Schmitzberger F, Kilkenny ML, Lobley CM, Webb ME, Vinkovic M, Matak-Vinkovic D, Witty M, Chirgadze DY, Smith AG, Abell C, Blundell TL EMBO J. 2003 Dec 1;22(23):6193-204. PMID:14633979<ref>PMID:14633979</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pqf" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Aspartate decarboxylase, which is translated as a pro-protein, undergoes intramolecular self-cleavage at Gly24-Ser25. We have determined the crystal structures of an unprocessed native precursor, in addition to Ala24 insertion, Ala26 insertion and Gly24--&gt;Ser, His11--&gt;Ala, Ser25--&gt;Ala, Ser25--&gt;Cys and Ser25--&gt;Thr mutants. Comparative analyses of the cleavage site reveal specific conformational constraints that govern self-processing and demonstrate that considerable rearrangement must occur. We suggest that Thr57 Ogamma and a water molecule form an 'oxyanion hole' that likely stabilizes the proposed oxyoxazolidine intermediate. Thr57 and this water molecule are probable catalytic residues able to support acid-base catalysis. The conformational freedom in the loop preceding the cleavage site appears to play a determining role in the reaction. The molecular mechanism of self-processing, presented here, emphasizes the importance of stabilization of the oxyoxazolidine intermediate. Comparison of the structural features shows significant similarity to those in other self-processing systems, and suggests that models of the cleavage site of such enzymes based on Ser--&gt;Ala or Ser--&gt;Thr mutants alone may lead to erroneous interpretations of the mechanism.
*[[Aspartate decarboxylase 3D structures|Aspartate decarboxylase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1PQF 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=1PQF OCA].
__TOC__
 
</StructureSection>
==Reference==
Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase., Schmitzberger F, Kilkenny ML, Lobley CM, Webb ME, Vinkovic M, Matak-Vinkovic D, Witty M, Chirgadze DY, Smith AG, Abell C, Blundell TL, EMBO J. 2003 Dec 1;22(23):6193-204. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14633979 14633979]
[[Category: Aspartate 1-decarboxylase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Abell, C.]]
[[Category: Abell C]]
[[Category: Blundell, T L.]]
[[Category: Blundell TL]]
[[Category: Chirgadze, D Y.]]
[[Category: Chirgadze DY]]
[[Category: Kilkenny, M L.]]
[[Category: Kilkenny ML]]
[[Category: Lobley, C M.C.]]
[[Category: Lobley CMC]]
[[Category: Matak-Vinkovic, D.]]
[[Category: Matak-Vinkovic D]]
[[Category: Schmitzberger, F.]]
[[Category: Schmitzberger F]]
[[Category: Smith, A G.]]
[[Category: Smith AG]]
[[Category: Vinkovic, M.]]
[[Category: Vinkovic M]]
[[Category: Webb, M E.]]
[[Category: Webb ME]]
[[Category: Witty, M.]]
[[Category: Witty M]]
[[Category: SO4]]
[[Category: intramolecular protein self-processing]]
[[Category: pyruvoyl-dependent decarboxylase]]
 
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Retrieved from "https://proteopedia.org/1pqf"