View source for 1tdp


==NMR solution structure of the carnobacteriocin B2 immunity protein==
<StructureSection load='1tdp' size='340' side='right'caption='[[1tdp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1tdp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Carnobacterium_maltaromaticum Carnobacterium maltaromaticum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TDP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1tdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tdp OCA], [https://pdbe.org/1tdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tdp RCSB], [https://www.ebi.ac.uk/pdbsum/1tdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tdp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CB2I_CARML CB2I_CARML] Could impart immunity to carnobacteriocin-B2 to naturally sensitive host strains.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteriocins produced by lactic acid bacteria are potent antimicrobial compounds which are active against closely related bacteria. Producer strains are protected against the effects of their cognate bacteriocins by immunity proteins that are located on the same genetic locus and are coexpressed with the gene encoding the bacteriocin. Several structures are available for class IIa bacteriocins; however, to date, no structures are available for the corresponding immunity proteins. We report here the NMR solution structure of the 111-amino acid immunity protein for carnobacteriocin B2 (ImB2). ImB2 folds into a globular domain in aqueous solution which contains an antiparallel four-helix bundle. Extensive packing by hydrophobic side chains in adjacent helices forms the core of the protein. The C-terminus, containing a fifth helix and an extended strand, is held against the four-helix bundle by hydrophobic interactions with helices 3 and 4. Most of the charged and polar residues in the protein face the solvent. Helix 3 is well-defined to residue 55, and a stretch of nascent helix followed by an unstructured loop joins it to helix 4. No interaction is observed between ImB2 and either carnobacteriocin B2 (CbnB2) or its precursor. Protection from the action of CbnB2 is only observed when ImB2 is expressed within the cell. The loop between helices 3 and 4, and a hydrophobic pocket which it partially masks, may be important for interaction with membrane receptors responsible for sensitivity to class IIa bacteriocins.

NMR solution structure of ImB2, a protein conferring immunity to antimicrobial activity of the type IIa bacteriocin, carnobacteriocin B2.,Sprules T, Kawulka KE, Vederas JC Biochemistry. 2004 Sep 21;43(37):11740-9. PMID:15362858<ref>PMID:15362858</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1tdp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Carnobacterium maltaromaticum]]
[[Category: Large Structures]]
[[Category: Kawulka KE]]
[[Category: Sprules T]]
[[Category: Vederas JC]]