2mlv

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==Structure of the antimicrobial peptide LsbB in TFE/water==
==Structure of the antimicrobial peptide LsbB in TFE/water==
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<StructureSection load='2mlv' size='340' side='right'caption='[[2mlv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2mlv' size='340' side='right'caption='[[2mlv]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2mlv]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MLV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2mlv]] 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=2MLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MLV FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mlu|2mlu]]</div></td></tr>
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</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=2mlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlv OCA], [https://pdbe.org/2mlv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mlv RCSB], [https://www.ebi.ac.uk/pdbsum/2mlv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlv ProSAT]</span></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=2mlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlv OCA], [https://pdbe.org/2mlv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mlv RCSB], [https://www.ebi.ac.uk/pdbsum/2mlv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlv ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q7X2B5_LACLL Q7X2B5_LACLL]
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LsbB is a class II leaderless lactococcal bacteriocin of 30 amino acids. In the present work, the structure and function relationship of LsbB was assessed. Structure determination by nuclear magnetic resonance (NMR) spectroscopy showed that LsbB has an N-terminal alpha-helix while the C-terminal of the molecule remains unstructured. To define the receptor binding domain of LsbB, a competition assay was performed in which a systematic collection of truncated peptides of various lengths covering different parts of LsbB was used to inhibit the antimicrobial activity of LsbB. The results indicate that the outmost eight amino acid sequence at the C-terminal end is likely to contain the receptor binding domain because only truncated fragments from this region could antagonize the antimicrobial activity of LsbB. Furthermore, alanine substitution revealed that the tryptophan in position 25 (W25) is crucial for the blocking activity of the truncated peptides as well as for the antimicrobial activity of the full-length bacteriocin. LsbB shares significant sequence homology with five other leaderless bacteriocins, especially at their C-terminal halves where all contain a conserved KxxxGxxPWE-motif, suggesting that they might recognize the same receptor as LsbB. This notion was supported by the fact that truncated peptides with sequences derived from the C-terminal regions of two LsbB-related bacteriocins inhibited the activity of LsbB, in the same manner as found with the truncated version of LsbB. Taken together these structure-function studies provide strong evidence that the receptor-binding parts of LsbB and sequence-related bacteriocins are located in their C-terminal halves.
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Defining the structure and receptor binding domain of the leaderless bacteriocin LsbB.,Ovchinnikov KV, Kristiansen PE, Uzelac G, Topisirovic L, Kojic M, Nissen-Meyer J, Nes IF, Diep DB J Biol Chem. 2014 Jul 3. pii: jbc.M114.579698. PMID:24993828<ref>PMID:24993828</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2mlv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lactococcus lactis subsp. lactis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Diep, D]]
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[[Category: Diep D]]
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[[Category: Kristiansen, P]]
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[[Category: Kristiansen P]]
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[[Category: Ovchinnikov, K]]
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[[Category: Ovchinnikov K]]
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[[Category: Antimicrobial peptide]]
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[[Category: Antimicrobial protein]]
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[[Category: Bacteriocin]]
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[[Category: Mode of killing]]
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[[Category: Receptor binding domain]]
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[[Category: Tfe]]
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Current revision

Structure of the antimicrobial peptide LsbB in TFE/water

PDB ID 2mlv

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