2hln: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==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=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2hln]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2hln]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_atrosepticus"_van_hall_1902 "bacillus atrosepticus" van hall 1902]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HLN FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zcf|1zcf]], [[2gvn|2gvn]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zcf|1zcf]], [[2gvn|2gvn]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lanS ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lanS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29471 "Bacillus atrosepticus" van Hall 1902])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hln OCA], [https://pdbe.org/2hln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hln RCSB], [https://www.ebi.ac.uk/pdbsum/2hln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hln ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 31: | Line 31: | ||
==See Also== | ==See Also== | ||
*[[Asparaginase|Asparaginase]] | *[[Asparaginase 3D structures|Asparaginase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 38: | Line 38: | ||
[[Category: Bacillus atrosepticus van hall 1902]] | [[Category: Bacillus atrosepticus van hall 1902]] | ||
[[Category: Asparaginase]] | [[Category: Asparaginase]] | ||
[[Category: Large Structures]] | |||
[[Category: Kislitsin, Y A]] | [[Category: Kislitsin, Y A]] | ||
[[Category: Kravchenko, O V]] | [[Category: Kravchenko, O V]] | ||
Revision as of 10:17, 24 March 2021
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
|
| ||||||||||||||||||||||