7byq: Difference between revisions
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==The mutant variant of PNGM-1. H279A was substituted for alanine to study metal coordination.== | ==The mutant variant of PNGM-1. H279A was substituted for alanine to study metal coordination.== | ||
<StructureSection load='7byq' size='340' side='right'caption='[[7byq]]' scene=''> | <StructureSection load='7byq' size='340' side='right'caption='[[7byq]], [[Resolution|resolution]] 1.96Å' 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=7BYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BYQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[7byq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BYQ 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=7byq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7byq OCA], [https://pdbe.org/7byq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7byq RCSB], [https://www.ebi.ac.uk/pdbsum/7byq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7byq 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=ZN:ZINC+ION'>ZN</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;'>[[6j4n|6j4n]]</div></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </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=7byq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7byq OCA], [https://pdbe.org/7byq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7byq RCSB], [https://www.ebi.ac.uk/pdbsum/7byq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7byq ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The increasing incidence of community- and hospital-acquired infections with multidrug-resistant (MDR) bacteria poses a critical threat to public health and the healthcare system. Although beta-lactam antibiotics are effective against most bacterial infections, some bacteria are resistant to beta-lactam antibiotics by producing beta-lactamases. Among beta-lactamases, metallo-beta-lactamases (MBLs) are especially worrisome as only a few inhibitors have been developed against them. In MBLs, the metal ions play an important role as they coordinate a catalytic water molecule that hydrolyzes beta-lactam rings. We determined the crystal structures of different variants of PNGM-1, an ancient MBL with additional tRNase Z activity. The variants were generated by site-directed mutagenesis targeting metal-coordinating residues. In PNGM-1, both zinc ions are coordinated by six coordination partners in an octahedral geometry, and the zinc-centered octahedrons share a common face. Structures of the PNGM-1 variants confirm that the substitution of a metal-coordinating residue causes the loss of metal binding and beta-lactamase activity. Compared with PNGM-1, subclass B3 MBLs lack one metal-coordinating residue, leading to a shift in the metal-coordination geometry from an octahedral to tetrahedral geometry. Our results imply that a subtle change in the metal-binding site of MBLs can markedly change their metal-coordination geometry and catalytic activity. | |||
Structural Study of Metal Binding and Coordination in Ancient Metallo-beta-Lactamase PNGM-1 Variants.,Park YS, Kim TY, Park H, Lee JH, Nguyen DQ, Hong MK, Lee SH, Kang LW Int J Mol Sci. 2020 Jul 12;21(14). pii: ijms21144926. doi: 10.3390/ijms21144926. PMID:32664695<ref>PMID:32664695</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7byq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Beta-lactamase]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kang | [[Category: Kang, L W]] | ||
[[Category: Lee | [[Category: Lee, J H]] | ||
[[Category: Park | [[Category: Park, Y S]] | ||
[[Category: Antibiotic]] | |||
[[Category: Mbl]] | |||
[[Category: Rnase z]] | |||
[[Category: Zinc binding motif]] | |||
Revision as of 09:09, 5 May 2021
The mutant variant of PNGM-1. H279A was substituted for alanine to study metal coordination.
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