2kyq
From Proteopedia
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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 | + | <StructureSection load='2kyq' size='340' side='right'caption='[[2kyq]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[2kyq]] is a 1 chain structure with sequence from [ | + | <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> |
| - | <b> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> |
| - | <b> | + | <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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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. | ||
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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<ref>PMID:21765060</ref> | 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<ref>PMID:21765060</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 2kyq" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Pentadiplandra brazzeana]] | [[Category: Pentadiplandra brazzeana]] | ||
| - | [[Category: Assadi-Porter | + | [[Category: Assadi-Porter FM]] |
| - | [[Category: Dittli | + | [[Category: Dittli SM]] |
| - | [[Category: Rao | + | [[Category: Rao H]] |
| - | [[Category: Tonelli | + | [[Category: Tonelli M]] |
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Current revision
1H, 15N, 13C chemical shifts and structure of CKR-brazzein
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