5ujq: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 5ujq is ON HOLD
+==NMR Solution Structure of the Two-component Bacteriocin CbnXY==
+<StructureSection load='5ujq' size='340' side='right'caption='[[5ujq]]' scene=''>
+== Structural highlights ==
+<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'>[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>
+== Function ==
+[https://www.uniprot.org/uniprot/Q46312_CARML Q46312_CARML]
+<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>
-[[Category: Miskolzie, M]]
+== References ==
-[[Category: Towle, K.M]]
+<references/>
-[[Category: Martin-Visscher, L.A.*]]
+__TOC__
-[[Category: Mckay, R.T]]
+</StructureSection>
-[[Category: Doerksen, T]]
+[[Category: Carnobacterium maltaromaticum]]
-[[Category: Acedo, J.Z]]
+[[Category: Large Structures]]
-[[Category: Vederas, J.C]]
+[[Category: Acedo JZ]]
+[[Category: Doerksen T]]
+[[Category: Lohans CT]]
+[[Category: Martin-Visscher LA]]
+[[Category: McKay RT]]
+[[Category: Miskolzie M]]
+[[Category: Towle KM]]
+[[Category: Vederas JC]]