7os6: Difference between revisions

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<StructureSection load='7os6' size='340' side='right'caption='[[7os6]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
<StructureSection load='7os6' size='340' side='right'caption='[[7os6]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
== 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'>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]] 1.43&#8491;</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>
== Function ==
[https://www.uniprot.org/uniprot/Q2K0Z2_RHIEC Q2K0Z2_RHIEC]
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7os6" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Asparaginase 3D structures|Asparaginase 3D structures]]
*[[Asparaginase 3D structures|Asparaginase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Rhizobium etli CFN 42]]
[[Category: Gilski M]]
[[Category: Gilski M]]
[[Category: Imiolczyk B]]
[[Category: Imiolczyk B]]
[[Category: Jaskolski M]]
[[Category: Jaskolski M]]
[[Category: Loch JI]]
[[Category: Loch JI]]

Latest revision as of 16:51, 6 November 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

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.43Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

7os6, resolution 1.43Å

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