4y68: Difference between revisions
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New page: '''Unreleased structure''' The entry 4y68 is ON HOLD Authors: Khosa, S., Hoeppner, A., Smits, S.H. Description: Structure of a lipoprotein from Streptococcus agalactiae [[Category: Unr... |
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The | ==Structure of a lipoprotein from Streptococcus agalactiae== | ||
<StructureSection load='4y68' size='340' side='right'caption='[[4y68]], [[Resolution|resolution]] 2.21Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4y68]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_515 Streptococcus agalactiae 515]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y68 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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=4y68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y68 OCA], [https://pdbe.org/4y68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y68 RCSB], [https://www.ebi.ac.uk/pdbsum/4y68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y68 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A140UHB6_STRAG A0A140UHB6_STRAG] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lantibiotics are potent antimicrobial peptides. Nisin is the most prominent member and contains five crucial lanthionine rings. Some clinically relevant bacteria express membrane-associated resistance proteins that proteolytically inactivate nisin. However, substrate recognition and specificity of these proteins is unknown. Here, we report the first three-dimensional structure of a nisin resistance protein from Streptococcus agalactiae (SaNSR) at 2.2 A resolution. It contains an N-terminal helical bundle, and protease cap and core domains. The latter harbors the highly conserved TASSAEM region, which lies in a hydrophobic tunnel formed by all domains. By integrative modeling, mutagenesis studies, and genetic engineering of nisin variants, a model of the SaNSR/nisin complex is generated, revealing that SaNSR recognizes the last C-terminally located lanthionine ring of nisin. This determines the substrate specificity of SaNSR and ensures the exact coordination of the nisin cleavage site at the TASSAEM region. | |||
Structural basis of lantibiotic recognition by the nisin resistance protein from Streptococcus agalactiae.,Khosa S, Frieg B, Mulnaes D, Kleinschrodt D, Hoeppner A, Gohlke H, Smits SH Sci Rep. 2016 Jan 4;6:18679. doi: 10.1038/srep18679. PMID:26727488<ref>PMID:26727488</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Hoeppner | <div class="pdbe-citations 4y68" style="background-color:#fffaf0;"></div> | ||
[[Category: Khosa | == References == | ||
[[Category: Smits | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus agalactiae 515]] | |||
[[Category: Hoeppner A]] | |||
[[Category: Khosa S]] | |||
[[Category: Smits SH]] | |||
