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| | ==1H, 15N, 13C chemical shifts and structure of CKR-brazzein== | | ==1H, 15N, 13C chemical shifts and structure of CKR-brazzein== |
| - | <StructureSection load='2kyq' size='340' side='right'caption='[[2kyq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kyq' size='340' side='right'caption='[[2kyq]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kyq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Penba Penba]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KYQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kyq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pentadiplandra_brazzeana Pentadiplandra brazzeana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KYQ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2kgq|2kgq]], [[1brz|1brz]]</div></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=2kyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kyq OCA], [https://pdbe.org/2kyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kyq RCSB], [https://www.ebi.ac.uk/pdbsum/2kyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kyq 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=2kyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kyq OCA], [https://pdbe.org/2kyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kyq RCSB], [https://www.ebi.ac.uk/pdbsum/2kyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kyq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/DEF_PENBA DEF_PENBA]] Taste-modifying protein; sweet-tasting. It is 2000 sweeter than sucrose on a molar basis.<ref>PMID:15118082</ref> Has a pH-specific antimicrobial activity against bacteria (B.subtilis, E.coli and S.aureus) and the fungus C.albicans.<ref>PMID:15118082</ref>
| + | [https://www.uniprot.org/uniprot/DEF_PENBA DEF_PENBA] Taste-modifying protein; sweet-tasting. It is 2000 sweeter than sucrose on a molar basis.<ref>PMID:15118082</ref> Has a pH-specific antimicrobial activity against bacteria (B.subtilis, E.coli and S.aureus) and the fungus C.albicans.<ref>PMID:15118082</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Penba]] | + | [[Category: Pentadiplandra brazzeana]] |
| - | [[Category: Assadi-Porter, F M]] | + | [[Category: Assadi-Porter FM]] |
| - | [[Category: Dittli, S M]] | + | [[Category: Dittli SM]] |
| - | [[Category: Rao, H]] | + | [[Category: Rao H]] |
| - | [[Category: Tonelli, M]] | + | [[Category: Tonelli M]] |
| - | [[Category: Plant protein]]
| + | |
| - | [[Category: Sweet-tasting protein]]
| + | |
| Structural highlights
Function
DEF_PENBA Taste-modifying protein; sweet-tasting. It is 2000 sweeter than sucrose on a molar basis.[1] Has a pH-specific antimicrobial activity against bacteria (B.subtilis, E.coli and S.aureus) and the fungus C.albicans.[2]
Publication Abstract from PubMed
Brazzein, a 54 residue sweet-tasting protein, is thought to participate in a multipoint binding interaction with the sweet taste receptor. Proposed sites for interaction with the receptor include 2 surface loops and the disulfide bond that connects the N- and C-termini. However, the importance of each site is not well understood. To characterize the structural role of the termini in the sweetness of brazzein, the position of the disulfide bond connecting the N- and C-termini was shifted by substituting K3-C4-K5 with C3-K4-R5. The apparent affinity and V(max) of the C3-K4-R5-brazzein (CKR-brazzein) variant were only modestly decreased compared with the wild-type (WT) brazzein. We determined a high-resolution structure of CKR-brazzein by nuclear magnetic resonance spectroscopy (backbone root mean square deviation of 0.39 A). Comparing the structure of CKR-brazzein with that of WT-brazzein revealed that the terminal beta-strands of the variant display extended beta-structure and increased dynamics relative to WT-brazzein. These results support previous mutagenesis studies and further suggest that, whereas interactions involving the termini are necessary for full function of brazzein, the termini do not constitute the primary site of interaction between brazzein and the sweet taste receptor.
Structural Role of the Terminal Disulfide Bond in the Sweetness of Brazzein.,Dittli SM, Rao H, Tonelli M, Quijada J, Markley JL, Max M, Assadi-Porter F Chem Senses. 2011 Jul 15. PMID:21765060[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yount NY, Yeaman MR. Multidimensional signatures in antimicrobial peptides. Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-8. Epub 2004 Apr 26. PMID:15118082 doi:10.1073/pnas.0401567101
- ↑ Yount NY, Yeaman MR. Multidimensional signatures in antimicrobial peptides. Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-8. Epub 2004 Apr 26. PMID:15118082 doi:10.1073/pnas.0401567101
- ↑ Dittli SM, Rao H, Tonelli M, Quijada J, Markley JL, Max M, Assadi-Porter F. Structural Role of the Terminal Disulfide Bond in the Sweetness of Brazzein. Chem Senses. 2011 Jul 15. PMID:21765060 doi:10.1093/chemse/bjr057
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