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==NMR Solution Structure of the Precursor for Carnobacteriocin B2, an Antimicrobial Peptide from Carnobacterium piscicola==
==NMR Solution Structure of the Precursor for Carnobacteriocin B2, an Antimicrobial Peptide from Carnobacterium piscicola==
<StructureSection load='1ry3' size='340' side='right'caption='[[1ry3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1ry3' size='340' side='right'caption='[[1ry3]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ry3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_27865 Atcc 27865]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RY3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ry3]] 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=1RY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RY3 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBNB2, CANCP52 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2751 ATCC 27865])</td></tr>
</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=1ry3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ry3 OCA], [https://pdbe.org/1ry3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ry3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ry3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ry3 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=1ry3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ry3 OCA], [https://pdbe.org/1ry3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ry3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ry3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ry3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CBB2_CARML CBB2_CARML]] Has antibacterial activity against Listeria and Enterococcus.  
[https://www.uniprot.org/uniprot/CBB2_CARML CBB2_CARML] Has antibacterial activity against Listeria and Enterococcus.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ry3 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ry3 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Type IIa bacteriocins, which are isolated from lactic acid bacteria that are useful for food preservation, are potent antimicrobial peptides with considerable potential as therapeutic agents for gastrointestinal infections in mammals. They are ribosomally synthesized as precursors with an N-terminal leader, typically 18-24 amino acid residues in length, which is cleaved during export from the producing cell. We have chemically synthesized the full precursor of carnobacteriocin B2, precarnobacteriocin (preCbnB2), which has a C-terminal amide rather than a carboxyl, and also produced preCbnB2(1-64), which is missing two amino acid residues at the C-terminus (Arg65 and Pro66), via expression in Escherichia coli as a maltose-binding protein fusion that is then cut with Factor Xa. PreCbnB2(1-64) is readily labeled with (15)N and (13)C for NMR studies using the latter approach. Multidimensional NMR analysis of preCbnB2(1-64) shows that, like the parent bacteriocin, it exists as a random coil in water but assumes a defined conformation in water/trifluoroethanol mixtures. In 70 : 30 trifluoroethanol/water, the 3D structure of the preCbnB2 section corresponding to the mature bacteriocin is essentially the same as reported previously by us for carnobacteriocin B2 (CbnB2). This structure maintains the highly conserved alpha-helix corresponding to residues 20-38 of CbnB2 that is believed to be responsible for interaction with a target receptor in sensitive cells, including Listeria monocytogenes. PreCbnB2 also has a second alpha-helix from residues 3-13 (i.e. -15 to -5 relative to CbnB2) in the leader section of the peptide. This helix appears to be conserved in related type IIa bacteriocin precursors based on sequence analysis. It is likely to be a key recognition element for export and processing, and is probably responsible for the considerably reduced antimicrobial activity of preCbnB2. The latter effect may assist the producing cell in avoiding the toxic effects of the bacteriocin. This is the first 3D structure determined for a prebacteriocin from lactic acid bacteria.
NMR solution structure of the precursor for carnobacteriocin B2, an antimicrobial peptide from Carnobacterium piscicola.,Sprules T, Kawulka KE, Gibbs AC, Wishart DS, Vederas JC Eur J Biochem. 2004 May;271(9):1748-56. PMID:15096213<ref>PMID:15096213</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ry3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 27865]]
[[Category: Carnobacterium maltaromaticum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gibbs, A C]]
[[Category: Gibbs AC]]
[[Category: Kawulka, K E]]
[[Category: Kawulka KE]]
[[Category: Sprules, T]]
[[Category: Sprules T]]
[[Category: Vederas, J C]]
[[Category: Vederas JC]]
[[Category: Wishart, D S]]
[[Category: Wishart DS]]
[[Category: Amphipathic helix]]
[[Category: Antibiotic]]

Revision as of 11:27, 1 May 2024

NMR Solution Structure of the Precursor for Carnobacteriocin B2, an Antimicrobial Peptide from Carnobacterium piscicolaNMR Solution Structure of the Precursor for Carnobacteriocin B2, an Antimicrobial Peptide from Carnobacterium piscicola

Structural highlights

1ry3 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.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBB2_CARML Has antibacterial activity against Listeria and Enterococcus.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Drag the structure with the mouse to rotate

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OCA
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