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4dy3

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dy3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DY3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dy3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DY3 FirstGlance]. <br>
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</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></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]] 1.8&#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></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=4dy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dy3 OCA], [https://pdbe.org/4dy3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dy3 RCSB], [https://www.ebi.ac.uk/pdbsum/4dy3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dy3 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=4dy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dy3 OCA], [https://pdbe.org/4dy3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dy3 RCSB], [https://www.ebi.ac.uk/pdbsum/4dy3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dy3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PLIG_ECOLI PLIG_ECOLI]] Inhibits activity of g-type lysozyme, which confers increased lysozyme tolerance to the bacterium.
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[https://www.uniprot.org/uniprot/PLIG_ECOLI PLIG_ECOLI] Inhibits activity of g-type lysozyme, which confers increased lysozyme tolerance to the bacterium.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Several Gram-negative bacteria protect themselves against the lytic action of host lysozymes by producing specific proteinaceous inhibitors. So far, four different families of lysozyme inhibitors have been identified including Ivy (Inhibitor of vertebrate lysozyme), MliC/PliC (Membrane associated/periplasmic inhibitor of C-type lysozyme), PliI and PliG (periplasmic inhibitors of I- and G-type lysozymes, respectively). Here we provide the first crystallographic description of the PliG family. Crystal structures were obtained for the PliG homologues from Escherichia coli, Salmonella enterica serotype Typhimurium and Aeromonas hydrophila. These structures show that the fold of the PliG family is very distinct from that of all other families of lysozyme inhibitors. Small-angle X-ray scattering studies reveal that PliG is monomeric in solution as opposed to the dimeric PliC and PliI. The PliG family shares a highly conserved SG(x)xY sequence motif with the MliC/PliC and PliI families where it was shown to reside on a loop that blocks the active site of lysozyme leading to inhibition. Surprisingly, we found that in PliG this motif is not well exposed and not involved in the inhibitory action. Instead, we could identify a distinct cluster of surface residues that are conserved across the PliG family and are essential for efficient G-type lysozyme inhibition, as evidenced by mutagenesis studies.
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Structural characterization of the PliG lysozyme inhibitor family.,Leysen S, Vanderkelen L, Asten KV, Vanheuverzwijn S, Theuwis V, Michiels CW, Strelkov SV J Struct Biol. 2012 May 24. PMID:22634186<ref>PMID:22634186</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 4dy3" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

crystal structure of Escherichia coli PliG, a periplasmic lysozyme inhibitor of g-type lysozyme

PDB ID 4dy3

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