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==L-asparaginase from Erwinia carotovora in complex with glutamic acid== | ==L-asparaginase from Erwinia carotovora in complex with glutamic acid== | ||
<StructureSection load='2hln' size='340' side='right' caption='[[2hln]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2hln' size='340' side='right' caption='[[2hln]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=2hln ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2hln" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Asparaginase|Asparaginase]] | *[[Asparaginase|Asparaginase]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:26, 26 February 2016
L-asparaginase from Erwinia carotovora in complex with glutamic acidL-asparaginase from Erwinia carotovora in complex with glutamic acid
Structural highlights
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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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