4y68: Difference between revisions
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''' | ==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y68 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y68 OCA], [http://pdbe.org/4y68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y68 RCSB], [http://www.ebi.ac.uk/pdbsum/4y68 PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
</div> | |||
<div class="pdbe-citations 4y68" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hoeppner, A]] | [[Category: Hoeppner, A]] | ||
[[Category: Khosa, S]] | [[Category: Khosa, S]] | ||
[[Category: Smits, S H]] | |||
[[Category: Hydrolase]] | |||
[[Category: Lantibiotic]] | |||
[[Category: Lipoprotein]] | |||
[[Category: Peptidase]] | |||
Revision as of 17:01, 20 January 2016
Structure of a lipoprotein from Streptococcus agalactiae
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