4pj2: Difference between revisions
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<StructureSection load='4pj2' size='340' side='right'caption='[[4pj2]], [[Resolution|resolution]] 1.24Å' scene=''> | <StructureSection load='4pj2' size='340' side='right'caption='[[4pj2]], [[Resolution|resolution]] 1.24Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4pj2]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4pj2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_hydrophila_subsp._hydrophila_ATCC_7966 Aeromonas hydrophila subsp. hydrophila ATCC 7966] and [https://en.wikipedia.org/wiki/Meretrix_lusoria Meretrix lusoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PJ2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene | </td></tr><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=MG:MAGNESIUM+ION'>MG</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=4pj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pj2 OCA], [https://pdbe.org/4pj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pj2 RCSB], [https://www.ebi.ac.uk/pdbsum/4pj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pj2 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/A0KHJ5_AERHH A0KHJ5_AERHH] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aeromonas hydrophila subsp. hydrophila ATCC 7966]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Meretrix lusoria]] | [[Category: Meretrix lusoria]] | ||
[[Category: Araki | [[Category: Araki T]] | ||
[[Category: Leysen S]] | |||
[[Category: Leysen | [[Category: Michiels CW]] | ||
[[Category: Michiels | [[Category: Ogata M]] | ||
[[Category: Ogata | [[Category: Strelkov SV]] | ||
[[Category: Strelkov | [[Category: Usui T]] | ||
[[Category: Usui | [[Category: Van Herreweghe JM]] | ||
[[Category: | [[Category: Yoneda K]] | ||
[[Category: | |||
Revision as of 16:07, 1 February 2023
Crystal structure of Aeromonas hydrophila PliI in complex with Meretrix lusoria lysozymeCrystal structure of Aeromonas hydrophila PliI in complex with Meretrix lusoria lysozyme
Structural highlights
FunctionPublication Abstract from PubMedRecent microbiological data have revealed that Gram-negative bacteria are able to protect themselves against the lytic action of host lysozymes by secreting proteinaceous inhibitors. Four distinct classes of such inhibitors have been discovered that specifically act against c-type, g-type and i-type lysozymes. Here, the 1.24 A resolution crystal structure of the periplasmic i-type lysozyme inhibitor from Aeromonas hydrophila (PliI-Ah) in complex with the i-type lysozyme from Meretrix lusoria is reported. The structure is the first to explain the inhibitory mechanism of the PliI family at the atomic level. A distinct `ridge' formed by three exposed PliI loops inserts into the substrate-binding groove of the lysozyme, resulting in a complementary `key-lock' interface. The interface is principally stabilized by the interactions made by the PliI-Ah residues Ser104 and Tyr107 belonging to the conserved SGxY motif, as well as by the other conserved residues Ser46 and Asp76. The functional importance of these residues is confirmed by inhibition assays with the corresponding point mutants of PliI-Ah. The accumulated structural data on lysozyme-inhibitor complexes from several classes indicate that in all cases an extensive interface of either a single or a double `key-lock' type is formed, resulting in highly efficient inhibition. These data provide a basis for the rational development of a new class of antibacterial drugs. The structure of the proteinaceous inhibitor PliI from Aeromonas hydrophila in complex with its target lysozyme.,Leysen S, Van Herreweghe JM, Yoneda K, Ogata M, Usui T, Araki T, Michiels CW, Strelkov SV Acta Crystallogr D Biol Crystallogr. 2015 Feb;71(Pt 2):344-51. doi:, 10.1107/S1399004714025863. Epub 2015 Jan 23. PMID:25664745[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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