5ujq: Difference between revisions

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==NMR Solution Structure of the Two-component Bacteriocin CbnXY==
==NMR Solution Structure of the Two-component Bacteriocin CbnXY==
<StructureSection load='5ujq' size='340' side='right'caption='[[5ujq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='5ujq' size='340' side='right'caption='[[5ujq]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ujq]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UJQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UJQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ujq]] 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=5UJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UJQ FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ujq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ujq OCA], [http://pdbe.org/5ujq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ujq RCSB], [http://www.ebi.ac.uk/pdbsum/5ujq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ujq ProSAT]</span></td></tr>
</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=5ujq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ujq OCA], [https://pdbe.org/5ujq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ujq RCSB], [https://www.ebi.ac.uk/pdbsum/5ujq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ujq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q46312_CARML Q46312_CARML]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Carnobacterium maltaromaticum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Acedo, J Z]]
[[Category: Acedo JZ]]
[[Category: Doerksen, T]]
[[Category: Doerksen T]]
[[Category: Lohans, C T]]
[[Category: Lohans CT]]
[[Category: Martin-Visscher, L A]]
[[Category: Martin-Visscher LA]]
[[Category: McKay, R T]]
[[Category: McKay RT]]
[[Category: Miskolzie, M]]
[[Category: Miskolzie M]]
[[Category: Towle, K M]]
[[Category: Towle KM]]
[[Category: Vederas, J C]]
[[Category: Vederas JC]]
[[Category: Antimicrobial protein]]

Latest revision as of 13:26, 14 June 2023

NMR Solution Structure of the Two-component Bacteriocin CbnXYNMR Solution Structure of the Two-component Bacteriocin CbnXY

Structural highlights

5ujq is a 1 chain structure with sequence from Carnobacterium maltaromaticum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q46312_CARML

Publication Abstract from PubMed

In this study, we report that CbnX (33 residues) and CbnY (29 residues) comprise a class IIb (two-component) bacteriocin in Carnobacteria. Individually, CbnX and CbnY are inactive, but together act synergistically to exert a narrow spectrum of activity. The structures of CbnX and CbnY in structure-inducing conditions were determined and strongly resemble other class IIb bacteriocins (i.e., LcnG, PlnEF, PlnJK). CbnX has an extended, amphipathic alpha-helix and a flexible C terminus. CbnY has two alpha-helices (one hydrophobic, one amphipathic) connected by a short loop and a cationic C terminus. CbnX and CbnY do not appear to interact directly and likely require a membrane-bound receptor to facilitate formation of the bacteriocin complex. This is the first class IIb bacteriocin reported for Carnobacteria.

Identification and three-dimensional structure of carnobacteriocin XY, a class IIb bacteriocin produced by Carnobacteria.,Acedo JZ, Towle KM, Lohans CT, Miskolzie M, McKay RT, Doerksen TA, Vederas JC, Martin-Visscher LA FEBS Lett. 2017 May;591(10):1349-1359. doi: 10.1002/1873-3468.12648. Epub 2017, Apr 27. PMID:28391617[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Acedo JZ, Towle KM, Lohans CT, Miskolzie M, McKay RT, Doerksen TA, Vederas JC, Martin-Visscher LA. Identification and three-dimensional structure of carnobacteriocin XY, a class IIb bacteriocin produced by Carnobacteria. FEBS Lett. 2017 May;591(10):1349-1359. doi: 10.1002/1873-3468.12648. Epub 2017, Apr 27. PMID:28391617 doi:http://dx.doi.org/10.1002/1873-3468.12648
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