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7luu

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==Kinetic and Structural Characterization of the First B3 Metallo-beta-Lactamase with an Active Site Glutamic Acid==
==Kinetic and Structural Characterization of the First B3 Metallo-beta-Lactamase with an Active Site Glutamic Acid==
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<StructureSection load='7luu' size='340' side='right'caption='[[7luu]]' scene=''>
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<StructureSection load='7luu' size='340' side='right'caption='[[7luu]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LUU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7luu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingobium_indicum_B90A Sphingobium indicum B90A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LUU FirstGlance]. <br>
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</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=7luu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7luu OCA], [https://pdbe.org/7luu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7luu RCSB], [https://www.ebi.ac.uk/pdbsum/7luu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7luu ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7luu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7luu OCA], [https://pdbe.org/7luu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7luu RCSB], [https://www.ebi.ac.uk/pdbsum/7luu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7luu ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A1L5BQA7_SPHIB A0A1L5BQA7_SPHIB]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structural diversity in metallo-beta-lactamases (MBLs), especially in the vicinity of the active site, has been a major hurdle in the development of clinically effective inhibitors. Representatives from three variants of the B3 MBL subclass, containing either the canonical HHH/DHH active-site motif (present in the majority of MBLs in this subclass) or the QHH/DHH (B3-Q) or HRH/DQK (B3-RQK) variations, were reported previously. Here, we describe the structure and kinetic properties of the first example (SIE-1) of a fourth variant containing the EHH/DHH active-site motif (B3-E). SIE-1 was identified in the hexachlorocyclohexane-degrading bacterium Sphingobium indicum, and kinetic analyses demonstrate that although it is active against a wide range of antibiotics, its efficiency is lower than that of other B3 MBLs but has increased efficiency toward cephalosporins relative to other beta-lactam substrates. The overall fold of SIE-1 is characteristic of the MBLs; the notable variation is observed in the Zn1 site due to the replacement of the canonical His116 by a glutamate. The unusual preference of SIE-1 for cephalosporins and its occurrence in a widespread environmental organism suggest the scope for increased MBL-mediated beta-lactam resistance. Thus, it is relevant to include SIE-1 in MBL inhibitor design studies to widen the therapeutic scope of much needed antiresistance drugs.
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Kinetic and Structural Characterization of the First B3 Metallo-beta-Lactamase with an Active-Site Glutamic Acid.,Wilson LA, Knaven EG, Morris MT, Monteiro Pedroso M, Schofield CJ, Bruck TB, Boden M, Waite DW, Hugenholtz P, Guddat L, Schenk G Antimicrob Agents Chemother. 2021 Sep 17;65(10):e0093621. doi:, 10.1128/AAC.00936-21. Epub 2021 Jul 26. PMID:34310207<ref>PMID:34310207</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7luu" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sphingobium indicum B90A]]
[[Category: Knaven E]]
[[Category: Knaven E]]
[[Category: Morris MT]]
[[Category: Morris MT]]
[[Category: Schenk G]]
[[Category: Schenk G]]
[[Category: Wilson L]]
[[Category: Wilson L]]

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Kinetic and Structural Characterization of the First B3 Metallo-beta-Lactamase with an Active Site Glutamic Acid

PDB ID 7luu

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