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| | ==Crystal structure of Gnk2 complexed with mannose== | | ==Crystal structure of Gnk2 complexed with mannose== |
| - | <StructureSection load='4xre' size='340' side='right' caption='[[4xre]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='4xre' size='340' side='right'caption='[[4xre]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xre]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XRE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xre]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ginkgo_biloba Ginkgo biloba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XRE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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]] 2.597Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a2e|3a2e]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></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=4xre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xre OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xre RCSB], [http://www.ebi.ac.uk/pdbsum/4xre PDBsum]</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=4xre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xre OCA], [https://pdbe.org/4xre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xre RCSB], [https://www.ebi.ac.uk/pdbsum/4xre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xre ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GNK2_GINBI GNK2_GINBI]] Possesses antifungal activity against F.oxysporum, T.reesei and C.albicans. Weakly inhibits the aspartic acid protease pepsin activity.<ref>PMID:17338634</ref> | + | [https://www.uniprot.org/uniprot/GNK2_GINBI GNK2_GINBI] Possesses antifungal activity against F.oxysporum, T.reesei and C.albicans. Weakly inhibits the aspartic acid protease pepsin activity.<ref>PMID:17338634</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4xre" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hatano, K]] | + | [[Category: Ginkgo biloba]] |
| - | [[Category: Miyakawa, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Miyauchi, Y]] | + | [[Category: Hatano K]] |
| - | [[Category: Sawano, Y]] | + | [[Category: Miyakawa T]] |
| - | [[Category: Suwa, Y]] | + | [[Category: Miyauchi Y]] |
| - | [[Category: Tanokura, M]] | + | [[Category: Sawano Y]] |
| - | [[Category: Antifungal activity]] | + | [[Category: Suwa Y]] |
| - | [[Category: Antifungal protein]] | + | [[Category: Tanokura M]] |
| - | [[Category: C-x8-c-x2-c motif]]
| + | |
| - | [[Category: Lectin]]
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| Structural highlights
Function
GNK2_GINBI Possesses antifungal activity against F.oxysporum, T.reesei and C.albicans. Weakly inhibits the aspartic acid protease pepsin activity.[1]
Publication Abstract from PubMed
Plants have a variety of mechanisms for defending against plant pathogens and tolerating environmental stresses such as drought and high salinity. Ginkbilobin2 (Gnk2) is a seed storage protein in gymnosperm that possesses antifungal activity and a plant-specific cysteine-rich motif (domain of unknown function26 [DUF26]). The Gnk2-homologous sequence is also observed in an extracellular region of cysteine-rich repeat receptor-like kinases that function in response to biotic and abiotic stresses. Here, we report the lectin-like molecular function of Gnk2 and the structural basis of its monosaccharide recognition. Nuclear magnetic resonance experiments showed that mannan was the only yeast (Saccharomyces cerevisiae) cell wall polysaccharide that interacted with Gnk2. Gnk2 also interacted with mannose, a building block of mannan, with a specificity that was similar to those of mannose-binding legume lectins, by strictly recognizing the configuration of the hydroxy group at the C4 position of the monosaccharide. The crystal structure of Gnk2 in complex with mannose revealed that three residues (asparagine-11, arginine-93, and glutamate-104) recognized mannose by hydrogen bonds, which defined the carbohydrate-binding specificity. These interactions were directly related to the ability of Gnk2 to inhibit the growth of fungi, including the plant pathogenic Fusarium spp., which were disrupted by mutation of arginine-93 or the presence of yeast mannan in the assay system. In addition, Gnk2 did not inhibit the growth of a yeast mutant strain lacking the alpha1,2-linked mannose moiety. These results provide insights into the molecular basis of the DUF26 protein family.
A secreted protein with plant-specific cysteine-rich motif functions as a mannose-binding lectin that exhibits antifungal activity.,Miyakawa T, Hatano K, Miyauchi Y, Suwa Y, Sawano Y, Tanokura M Plant Physiol. 2014 Oct;166(2):766-78. doi: 10.1104/pp.114.242636. Epub 2014 Aug , 19. PMID:25139159[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sawano Y, Miyakawa T, Yamazaki H, Tanokura M, Hatano K. Purification, characterization, and molecular gene cloning of an antifungal protein from Ginkgo biloba seeds. Biol Chem. 2007 Mar;388(3):273-80. PMID:17338634 doi:http://dx.doi.org/10.1515/BC.2007.030
- ↑ Miyakawa T, Hatano K, Miyauchi Y, Suwa Y, Sawano Y, Tanokura M. A secreted protein with plant-specific cysteine-rich motif functions as a mannose-binding lectin that exhibits antifungal activity. Plant Physiol. 2014 Oct;166(2):766-78. doi: 10.1104/pp.114.242636. Epub 2014 Aug , 19. PMID:25139159 doi:http://dx.doi.org/10.1104/pp.114.242636
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