View source for 5lfi


==lactococcin A immunity protein==
<StructureSection load='5lfi' size='340' side='right'caption='[[5lfi]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lfi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis Lactococcus lactis subsp. lactis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LFI 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=5lfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfi OCA], [https://pdbe.org/5lfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lfi RCSB], [https://www.ebi.ac.uk/pdbsum/5lfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LCIA_LACLL LCIA_LACLL] Imparts immunity to lactococcin-A to naturally sensitive host strains.
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== Publication Abstract from PubMed ==
The class IId bacteriocin lactococcin A and the pediocin-like bacteriocins induce membrane leakage and cell death by specifically binding the mannose phophotransferase system (man-PTS) on their target cells. The bacteriocins' cognate immunity proteins that protect the producer cell from its own bacteriocin recognize and bind to the bacteriocin-man-PTS complex and thereby block membrane leakage. In this study, we have determined the three-dimensional structure of the lactococcin A immunity protein (LciA) by the use of nuclear magnetic resonance spectroscopy. LciA forms a four-helix bundle structure with a flexible C-terminal tail. Despite the low degree of sequence similarity between LciA and the pediocin-like immunity proteins, they share the same fold. However, there are certain differences between the structures. The C-terminal helix in LciA is considerably shorter than that observed in the pediocin-like immunity proteins, and the surface potentials of the immunity proteins differ. Truncated variants of LciA in which 6 or 10 of the C-terminal residues were removed yielded a reduced degree of protection, indicating that the unstructured C-terminal tail is important for the functionality of the immunity proteins.

Nuclear Magnetic Resonance Structure and Mutational Analysis of the Lactococcin A Immunity Protein.,Kristiansen PE, Persson C, Fuochi V, Pedersen A, Karlsson GB, Nissen-Meyer J, Oppegard C Biochemistry. 2016 Nov 3. PMID:27808503<ref>PMID:27808503</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5lfi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactococcus lactis subsp. lactis]]
[[Category: Large Structures]]
[[Category: Fuochi V]]
[[Category: Karlsson BG]]
[[Category: Kristiansen PE]]
[[Category: Nissen-Meyer J]]
[[Category: Oppegard C]]
[[Category: Pedersen A]]
[[Category: Persson C]]