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==Crystal structure of Rhizobium etli inducible L-asparaginase ReAV (orthorhombic form OP)== | ==Crystal structure of Rhizobium etli inducible L-asparaginase ReAV (orthorhombic form OP)== | ||
<StructureSection load='7os5' size='340' side='right'caption='[[7os5]]' scene=''> | <StructureSection load='7os5' size='340' side='right'caption='[[7os5]], [[Resolution|resolution]] 1.29Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OS5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7os5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OS5 FirstGlance]. <br> | ||
</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=7os5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7os5 OCA], [https://pdbe.org/7os5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7os5 RCSB], [https://www.ebi.ac.uk/pdbsum/7os5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7os5 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7os3|7os3]], [[7os6|7os6]], [[7ou1|7ou1]]</div></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=7os5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7os5 OCA], [https://pdbe.org/7os5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7os5 RCSB], [https://www.ebi.ac.uk/pdbsum/7os5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7os5 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rhizobium etli, a nitrogen-fixing bacterial symbiont of legume plants, encodes an essential L-asparaginase (ReAV) with no sequence homology to known enzymes with this activity. High-resolution crystal structures of ReAV show indeed a structurally distinct, dimeric enzyme, with some resemblance to glutaminases and beta-lactamases. However, ReAV has no glutaminase or lactamase activity, and at pH 9 its allosteric asparaginase activity is relatively high, with Km for L-Asn at 4.2 mM and kcat of 438 s(-1). The active site of ReAV, deduced from structural comparisons and confirmed by mutagenesis experiments, contains a highly specific Zn(2+) binding site without a catalytic role. The extensive active site includes residues with unusual chemical properties. There are two Ser-Lys tandems, all connected through a network of H-bonds to the Zn center, and three tightly bound water molecules near Ser48, which clearly indicate the catalytic nucleophile. | |||
Crystal structures of the elusive Rhizobium etli L-asparaginase reveal a peculiar active site.,Loch JI, Imiolczyk B, Sliwiak J, Wantuch A, Bejger M, Gilski M, Jaskolski M Nat Commun. 2021 Nov 18;12(1):6717. doi: 10.1038/s41467-021-27105-x. PMID:34795296<ref>PMID:34795296</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7os5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gilski M]] | [[Category: Gilski, M]] | ||
[[Category: Imiolczyk B]] | [[Category: Imiolczyk, B]] | ||
[[Category: Jaskolski M]] | [[Category: Jaskolski, M]] | ||
[[Category: Loch | [[Category: Loch, J I]] | ||
[[Category: Amidohydrolase]] | |||
[[Category: Hydrolase]] | |||
[[Category: L-asparaginase]] | |||
[[Category: Rhizobium etli]] | |||
Revision as of 09:31, 1 December 2021
Crystal structure of Rhizobium etli inducible L-asparaginase ReAV (orthorhombic form OP)Crystal structure of Rhizobium etli inducible L-asparaginase ReAV (orthorhombic form OP)
Structural highlights
Publication Abstract from PubMedRhizobium etli, a nitrogen-fixing bacterial symbiont of legume plants, encodes an essential L-asparaginase (ReAV) with no sequence homology to known enzymes with this activity. High-resolution crystal structures of ReAV show indeed a structurally distinct, dimeric enzyme, with some resemblance to glutaminases and beta-lactamases. However, ReAV has no glutaminase or lactamase activity, and at pH 9 its allosteric asparaginase activity is relatively high, with Km for L-Asn at 4.2 mM and kcat of 438 s(-1). The active site of ReAV, deduced from structural comparisons and confirmed by mutagenesis experiments, contains a highly specific Zn(2+) binding site without a catalytic role. The extensive active site includes residues with unusual chemical properties. There are two Ser-Lys tandems, all connected through a network of H-bonds to the Zn center, and three tightly bound water molecules near Ser48, which clearly indicate the catalytic nucleophile. Crystal structures of the elusive Rhizobium etli L-asparaginase reveal a peculiar active site.,Loch JI, Imiolczyk B, Sliwiak J, Wantuch A, Bejger M, Gilski M, Jaskolski M Nat Commun. 2021 Nov 18;12(1):6717. doi: 10.1038/s41467-021-27105-x. PMID:34795296[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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