5yh4: Difference between revisions
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<StructureSection load='5yh4' size='340' side='right' caption='[[5yh4]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='5yh4' size='340' side='right' caption='[[5yh4]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5yh4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YH4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YH4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5yh4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Grape Grape]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YH4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YH4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VITISV_025776 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29760 Grape])</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=5yh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yh4 OCA], [http://pdbe.org/5yh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yh4 RCSB], [http://www.ebi.ac.uk/pdbsum/5yh4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yh4 ProSAT]</span></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=5yh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yh4 OCA], [http://pdbe.org/5yh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yh4 RCSB], [http://www.ebi.ac.uk/pdbsum/5yh4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yh4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The so-called miraculin-like proteins (MLPs) are homologous to miraculin, a homodimeric protein with taste-modifying activity that converts sourness into sweetness. The identity between MLPs and miraculin generally ranges from 30% to 55%, and both MLPs and miraculin are categorized into the Kunitz-type soybean trypsin inhibitor (STI) family. MLP from grape (Vitis vinifera; vvMLP) exhibits significant homology to miraculin (61% identity), suggesting that vvMLP possesses miraculin-like properties. The results of size-exclusion chromatography and sensory analysis illustrated that vvMLP exists as a monomer in solution with no detectable taste-modifying activity. Crystal structure determination revealed that vvMLP exists as a beta-trefoil fold, similarly as other MLPs and Kunitz-type protein inhibitors. The conformation of the loops, including the so-called reactive loop in the STI family, was substantially different between vvMLP and STI. Recombinant vvMLP had inhibitory activity against trypsin (Ki=13.7muM), indicating that the protein can act as a moderate trypsin inhibitor. | |||
Structural and functional analysis of miraculin-like protein from Vitis vinifera.,Ohkura SI, Hori M, Saitoh K, Okuzawa T, Okamoto I, Furukawa N, Shimizu-Ibuka A Biochim Biophys Acta Proteins Proteom. 2018 Nov;1866(11):1125-1130. doi:, 10.1016/j.bbapap.2018.08.009. Epub 2018 Aug 27. PMID:30282610<ref>PMID:30282610</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5yh4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Grape]] | |||
[[Category: Furukawa, N]] | [[Category: Furukawa, N]] | ||
[[Category: Shimizu-Ibuka, A]] | [[Category: Shimizu-Ibuka, A]] | ||
Revision as of 11:30, 17 October 2018
Miraculin-like protein from Vitis viniferaMiraculin-like protein from Vitis vinifera
Structural highlights
Publication Abstract from PubMedThe so-called miraculin-like proteins (MLPs) are homologous to miraculin, a homodimeric protein with taste-modifying activity that converts sourness into sweetness. The identity between MLPs and miraculin generally ranges from 30% to 55%, and both MLPs and miraculin are categorized into the Kunitz-type soybean trypsin inhibitor (STI) family. MLP from grape (Vitis vinifera; vvMLP) exhibits significant homology to miraculin (61% identity), suggesting that vvMLP possesses miraculin-like properties. The results of size-exclusion chromatography and sensory analysis illustrated that vvMLP exists as a monomer in solution with no detectable taste-modifying activity. Crystal structure determination revealed that vvMLP exists as a beta-trefoil fold, similarly as other MLPs and Kunitz-type protein inhibitors. The conformation of the loops, including the so-called reactive loop in the STI family, was substantially different between vvMLP and STI. Recombinant vvMLP had inhibitory activity against trypsin (Ki=13.7muM), indicating that the protein can act as a moderate trypsin inhibitor. Structural and functional analysis of miraculin-like protein from Vitis vinifera.,Ohkura SI, Hori M, Saitoh K, Okuzawa T, Okamoto I, Furukawa N, Shimizu-Ibuka A Biochim Biophys Acta Proteins Proteom. 2018 Nov;1866(11):1125-1130. doi:, 10.1016/j.bbapap.2018.08.009. Epub 2018 Aug 27. PMID:30282610[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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