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| | ==Crystal structure of mabinlin II== | | ==Crystal structure of mabinlin II== |
| - | <StructureSection load='2ds2' size='340' side='right' caption='[[2ds2]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='2ds2' size='340' side='right'caption='[[2ds2]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ds2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Capparis_masaikai Capparis masaikai]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DS2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DS2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ds2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Capparis_masaikai Capparis masaikai]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DS2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</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=2ds2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ds2 OCA], [http://pdbe.org/2ds2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ds2 RCSB], [http://www.ebi.ac.uk/pdbsum/2ds2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ds2 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></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=2ds2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ds2 OCA], [https://pdbe.org/2ds2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ds2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ds2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ds2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/2SS2_CAPMA 2SS2_CAPMA]] Heat stable 2S seed storage protein having sweetness-inducing activity. | + | [https://www.uniprot.org/uniprot/2SS2_CAPMA 2SS2_CAPMA] Heat stable 2S seed storage protein having sweetness-inducing activity. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/2ds2_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/2ds2_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Capparis masaikai]] | | [[Category: Capparis masaikai]] |
| - | [[Category: Li, D F]] | + | [[Category: Large Structures]] |
| - | [[Category: Wang, D C]] | + | [[Category: Li DF]] |
| - | [[Category: Zhu, D Y]] | + | [[Category: Wang DC]] |
| - | [[Category: Plant protein]] | + | [[Category: Zhu DY]] |
| - | [[Category: Seed storage protein]]
| + | |
| - | [[Category: Sweet protein]]
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| Structural highlights
Function
2SS2_CAPMA Heat stable 2S seed storage protein having sweetness-inducing activity.
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
The crystal structure of a sweet protein Mabinlin II (Mab II) isolated from the mature seeds of Capparis masaikai Levl. grown in Southern China has been determined at 1.7A resolution by the SIRAS method. The Mab II 3D structure features in an "all alpha" fold mode consisting of A- and B-chains crosslinked by four disulfide bridges, which is distinct from all known sweet protein structures. The Mabinlin II molecule shows an amphiphilic surface, a cationic face (Face A) and a neutral face (Face B). A unique structural motif consisting of B54-B64 was found in Face B, which adopts a special sequence, NL-P-NI-C-NI-P-NI, featuring four [Asn-Leu/Ile] units connected by three conformational-constrained residues, thus is called the [NL/I] tetralet motif. The experiments for testing the possible interactions of separated A-chain and B-chain and the native Mabinlin II to the sweet-taste receptor were performed through the calcium imaging experiments with the HEK293E cells coexpressed hT1R2/T1R3. The result shows that hT1R2/T1R3 responds to both the integrated Mabinlin II and the individual B-chain in the same scale, but not to A-chain. The sweetness evaluation further identified that the separated B-chain can elicit the sweetness alone, but A-chain does not. All data in combination revealed that the sweet protein Mabinlin II can interact with the sweet-taste receptor hT1R2/T1R3 to elicit its sweet taste, and the B-chain with a unique [NL/I] tetralet motif is the essential structural element for the interaction with sweet-taste receptor to elicit the sweetness, while the A-chain may play a role in gaining a long aftertaste for the integrate Mabinlin II. The findings reported in this paper will be advantage for understanding the diversity of sweet proteins and engineering research for development of a unique sweetener for the food and agriculture based on the Mabinlin II structure as a native model.
Crystal structure of Mabinlin II: a novel structural type of sweet proteins and the main structural basis for its sweetness.,Li DF, Jiang P, Zhu DY, Hu Y, Max M, Wang DC J Struct Biol. 2008 Apr;162(1):50-62. Epub 2008 Jan 11. PMID:18308584[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li DF, Jiang P, Zhu DY, Hu Y, Max M, Wang DC. Crystal structure of Mabinlin II: a novel structural type of sweet proteins and the main structural basis for its sweetness. J Struct Biol. 2008 Apr;162(1):50-62. Epub 2008 Jan 11. PMID:18308584 doi:10.1016/j.jsb.2007.12.007
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