View source for 2gvn


==L-asparaginase from Erwinia carotovora in complex with aspartic acid==
<StructureSection load='2gvn' size='340' side='right'caption='[[2gvn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2gvn]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_atrosepticum Pectobacterium atrosepticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GVN 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</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=2gvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gvn OCA], [https://pdbe.org/2gvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gvn RCSB], [https://www.ebi.ac.uk/pdbsum/2gvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gvn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I1SBD9_PECAS I1SBD9_PECAS] 
== 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/gv/2gvn_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=2gvn ConSurf].
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== Publication Abstract from PubMed ==
The crystal structures of Erwinia carotovora L-asparaginase complexed with L-aspartate and L-glutamate were determined at 1.9 and 2.2 A, respectively, using the molecular-replacement method and were refined to R factors of about 21% in both cases. The positions of the ligands in the active site were located. A comparison of the new structures with the known structures of Escherichia coli L-asparaginase and Er. chrysanthemi L-asparaginase was performed. It was found that the arrangement of the ligands practically coincides in all three enzymes. The peculiarities of the quaternary structure of the enzyme, the possible role of water molecules in the enzyme action and the conformational changes during the catalyzed reaction are discussed.

Three-dimensional structures of L-asparaginase from Erwinia carotovora complexed with aspartate and glutamate.,Kravchenko OV, Kislitsin YA, Popov AN, Nikonov SV, Kuranova IP Acta Crystallogr D Biol Crystallogr. 2008 Mar;64(Pt 3):248-56. doi:, 10.1107/S0907444907065766. Epub 2008 Feb 20. PMID:18323619<ref>PMID:18323619</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2gvn" style="background-color:#fffaf0;"></div>

==See Also==
*[[Asparaginase 3D structures|Asparaginase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pectobacterium atrosepticum]]
[[Category: Kislitsin YA]]
[[Category: Kravchenko OV]]
[[Category: Kuranova IP]]
[[Category: Nikonov SV]]
[[Category: Popov AN]]