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| | ==NMR solution structure of PisI== | | ==NMR solution structure of PisI== |
| - | <StructureSection load='2k19' size='340' side='right' caption='[[2k19]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2k19' size='340' side='right'caption='[[2k19]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2k19]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Carnobacterium_maltaromaticum Carnobacterium maltaromaticum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K19 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2k19]] 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=2K19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K19 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pisI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2751 Carnobacterium maltaromaticum])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k19 OCA], [http://pdbe.org/2k19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k19 RCSB], [http://www.ebi.ac.uk/pdbsum/2k19 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k19 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=2k19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k19 OCA], [https://pdbe.org/2k19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k19 RCSB], [https://www.ebi.ac.uk/pdbsum/2k19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k19 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2VU68_CARML Q2VU68_CARML] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Carnobacterium maltaromaticum]] | | [[Category: Carnobacterium maltaromaticum]] |
| - | [[Category: Gursky, L J]] | + | [[Category: Large Structures]] |
| - | [[Category: Martin-Visscher, L A]] | + | [[Category: Gursky LJ]] |
| - | [[Category: Sprules, T]] | + | [[Category: Martin-Visscher LA]] |
| - | [[Category: Vederas, J C]] | + | [[Category: Sprules T]] |
| - | [[Category: Antimicrobial protein]]
| + | [[Category: Vederas JC]] |
| - | [[Category: Bacteriocin]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Immunity protein]]
| + | |
| - | [[Category: Pisi]]
| + | |
| Structural highlights
Function
Q2VU68_CARML
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Lactic acid bacteria produce and secrete bacteriocins. These bacteriocins are potent antimicrobial peptides that are active against other closely related bacteria. As a means of self-protection, producer organisms also express immunity proteins. Immunity proteins are generally located on the same genetic locus and are cotranscribed with the bacteriocin. Although some cross immunity between bacteriocins has been observed, immunity proteins are typically highly specific. Immunity proteins for the type IIa bacteriocins range from 81 to 115 amino acids in length and display substantial variation in their sequences. Nonetheless, such immunity proteins have been classified into three groupings (groups A, B, and C) according to sequence homology. The structures of a group C (ImB2) and two group A (EntA-im and PedB) immunity proteins have previously been reported. We herein report the nuclear magnetic resonance solution structure of the remaining class of the type IIa immunity proteins. PisI, a 98-amino acid protein, is a group B immunity protein conferring immunity against piscicolin 126 (PisA). Like ImB2, EntA-im, and PedB, PisI folds into a globular protein in aqueous solution and contains an antiparallel four-helix bundle. Compared to ImB2 and EntA-im, PisI has a substantially longer and more flexbile N-terminus, but a shorter C-terminus. No direct interaction between the bacteriocin and immunity protein is observed by NMR in either aqueous or membrane mimicking environments. This further suggests that the mechanism that mediates immunity is not due to a direct bacteriocin-immunity protein interaction but rather is receptor-mediated. It has now been confirmed that the four-helix bundle is indeed a structural motif among the type IIa immunity proteins.
Nuclear magnetic resonance solution structure of PisI, a group B immunity protein that provides protection against the type IIa bacteriocin piscicolin 126, PisA.,Martin-Visscher LA, Sprules T, Gursky LJ, Vederas JC Biochemistry. 2008 Jun 17;47(24):6427-36. Epub 2008 May 24. PMID:18500825[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Martin-Visscher LA, Sprules T, Gursky LJ, Vederas JC. Nuclear magnetic resonance solution structure of PisI, a group B immunity protein that provides protection against the type IIa bacteriocin piscicolin 126, PisA. Biochemistry. 2008 Jun 17;47(24):6427-36. Epub 2008 May 24. PMID:18500825 doi:10.1021/bi8004076
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