2ly6: Difference between revisions

Revision as of 09:21, 14 June 2023

Refined solution structure of recombinant brazzein at low temperature

Structural highlights

2ly6 is a 1 chain structure with sequence from Pentadiplandra brazzeana. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

The sweet protein brazzein, a member of the Csbetaalpha fold family, contains four disulfide bonds that lend a high degree of thermal and pH stability to its structure. Nevertheless, a variable temperature study has revealed that the protein undergoes a local, reversible conformational change between 37 degrees C and 3 degrees C with a midpoint about 27 degrees C that changes the orientations and side-chain hydrogen bond partners of Tyr8 and Tyr11. To test the functional significance of this effect, we used NMR saturation transfer to investigate the interaction between brazzein and the amino terminal domain (ATD) of the sweet receptor subunit T1R2; the results showed a stronger interaction at 7 degrees C than at 37 degrees C. Thus the low temperature conformation, which alters the orientations of two loops known to be critical for the sweetness of brazzein, may represent the bound state of brazzein in the complex with the human sweet receptor. Proteins 2013. (c) 2013 Wiley Periodicals, Inc.

Temperature-dependent conformational change affecting Tyr11 and sweetness loops of brazzein.,Cornilescu CC, Cornilescu G, Rao H, Porter SF, Tonelli M, Derider ML, Markley JL, Assadi-Porter FM Proteins. 2013 Jan 24. doi: 10.1002/prot.24259. PMID:23349025^[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
↑ Cornilescu CC, Cornilescu G, Rao H, Porter SF, Tonelli M, Derider ML, Markley JL, Assadi-Porter FM. Temperature-dependent conformational change affecting Tyr11 and sweetness loops of brazzein. Proteins. 2013 Jan 24. doi: 10.1002/prot.24259. PMID:23349025 doi:10.1002/prot.24259

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] Cornilescu CC, Cornilescu G, Rao H, Porter SF, Tonelli M, Derider ML, Markley JL, Assadi-Porter FM. Temperature-dependent conformational change affecting Tyr11 and sweetness loops of brazzein. Proteins. 2013 Jan 24. doi: 10.1002/prot.24259. PMID:23349025 doi:10.1002/prot.24259

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
 ==Refined solution structure of recombinant brazzein at low temperature==
-<StructureSection load='2ly6' size='340' side='right'caption='[[2ly6]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
+<StructureSection load='2ly6' size='340' side='right'caption='[[2ly6]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ly6]] 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=2LY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LY6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ly6]] 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=2LY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LY6 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;'>[[2ly5|2ly5]]</div></td></tr>
+</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=2ly6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ly6 OCA], [https://pdbe.org/2ly6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ly6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ly6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ly6 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=2ly6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ly6 OCA], [https://pdbe.org/2ly6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ly6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ly6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ly6 ProSAT]</span></td></tr>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Penba]]
+[[Category: Pentadiplandra brazzeana]]
-[[Category: Assadi-Porter, F M]]
+[[Category: Assadi-Porter FM]]
-[[Category: Cornilescu, C C]]
+[[Category: Cornilescu CC]]
-[[Category: Cornilescu, G]]
+[[Category: Cornilescu G]]
-[[Category: Markley, J L]]
+[[Category: Markley JL]]
-[[Category: Tonelli, M]]
+[[Category: Tonelli M]]
-[[Category: Brazzein]]
-[[Category: Cys-sail]]
-[[Category: Plant protein]]

2ly6: Difference between revisions

Revision as of 09:21, 14 June 2023

Refined solution structure of recombinant brazzein at low temperature

Structural highlights

Function

Publication Abstract from PubMed

References

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