7os6: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7os6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_etli_CFN_42 Rhizobium etli CFN 42]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OS6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7os6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_etli_CFN_42 Rhizobium etli CFN 42]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OS6 FirstGlance]. <br> | ||
</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=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.43Å</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=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7os6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7os6 OCA], [https://pdbe.org/7os6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7os6 RCSB], [https://www.ebi.ac.uk/pdbsum/7os6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7os6 ProSAT]</span></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=7os6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7os6 OCA], [https://pdbe.org/7os6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7os6 RCSB], [https://www.ebi.ac.uk/pdbsum/7os6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7os6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Revision as of 14:16, 2 May 2024
Crystal structure of Rhizobium etli inducible L-asparaginase ReAV (monoclinic form MP1)Crystal structure of Rhizobium etli inducible L-asparaginase ReAV (monoclinic form MP1)
Structural highlights
FunctionPublication 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. See AlsoReferences
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