5lfi: Difference between revisions
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The | ==lactococcin A immunity protein== | ||
<StructureSection load='5lfi' size='340' side='right' caption='[[5lfi]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5lfi]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LFI FirstGlance]. <br> | |||
</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=5lfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfi OCA], [http://pdbe.org/5lfi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lfi RCSB], [http://www.ebi.ac.uk/pdbsum/5lfi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfi ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/LCIA_LACLL LCIA_LACLL]] Imparts immunity to lactococcin-A to naturally sensitive host strains. | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5lfi" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Fuochi, V]] | [[Category: Fuochi, V]] | ||
[[Category: Kristiansen, P | [[Category: Karlsson, B G]] | ||
[[Category: Kristiansen, P E]] | |||
[[Category: Nissen-Meyer, J]] | |||
[[Category: Oppegard, C]] | |||
[[Category: Pedersen, A]] | [[Category: Pedersen, A]] | ||
[[Category: Persson, C]] | [[Category: Persson, C]] | ||
[[Category: | [[Category: Bacteriocin receptor]] | ||
[[Category: | [[Category: Four-helix bundle]] | ||
[[Category: Immune system]] | |||
[[Category: Immunity protein]] | |||
Revision as of 03:29, 10 December 2016
lactococcin A immunity protein
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