5ujq: Difference between revisions

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'''Unreleased structure'''


The entry 5ujq is ON HOLD  until Paper Publication
==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=''>
== 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://oca.weizmann.ac.il/oca-docs/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://oca.weizmann.ac.il/oca-docs/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>
</table>
<div style="background-color:#fffaf0;">
== 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.


Authors: Acedo, J.Z., Towle, K.M., Lohans, C.T., McKay, R.T., Miskolzie, M., Doerksen, T., Vederas, J.C., Martin-Visscher, L.A.
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<ref>PMID:28391617</ref>


Description: NMR Solution Structure of the Two-component Bacteriocin CbnXY
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Lohans, C.T]]
<div class="pdbe-citations 5ujq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acedo, J Z]]
[[Category: Doerksen, T]]
[[Category: Lohans, C T]]
[[Category: Martin-Visscher, L A]]
[[Category: McKay, R T]]
[[Category: Miskolzie, M]]
[[Category: Miskolzie, M]]
[[Category: Towle, K.M]]
[[Category: Towle, K M]]
[[Category: Mckay, R.T]]
[[Category: Vederas, J C]]
[[Category: Doerksen, T]]
[[Category: Antimicrobial protein]]
[[Category: Acedo, J.Z]]
[[Category: Martin-Visscher, L.A]]
[[Category: Vederas, J.C]]

Revision as of 09:11, 29 November 2017

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. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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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