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| | <StructureSection load='4mst' size='340' side='right'caption='[[4mst]], [[Resolution|resolution]] 1.93Å' scene=''> | | <StructureSection load='4mst' size='340' side='right'caption='[[4mst]], [[Resolution|resolution]] 1.93Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4mst]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hevbr Hevbr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MST OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MST FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4mst]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hevea_brasiliensis Hevea brasiliensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MST FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mpi|4mpi]]</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=4mst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mst OCA], [https://pdbe.org/4mst PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mst RCSB], [https://www.ebi.ac.uk/pdbsum/4mst PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mst ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hbchi-L1, rq30 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3981 HEVBR])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </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=4mst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mst OCA], [http://pdbe.org/4mst PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mst RCSB], [http://www.ebi.ac.uk/pdbsum/4mst PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mst ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CHI1_HEVBR CHI1_HEVBR] Inactive chitinase-like protein that does not exhibit hydrolytic activity toward chitin (PubMed:25104038). Binds strongly to chitin and possesses antifungal activity toward the fungal pathogen Altenaria alternata in plate assays (PubMed:25104038). Inhibits the growth of Fusarium oxysporum on plate assays (PubMed:11940078). Probably involved in defense against fungal pathogens through a mechanism that only involves carbohydrate binding (PubMed:25104038).<ref>PMID:11940078</ref> <ref>PMID:25104038</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Chitinase|Chitinase]] | + | *[[Chitinase 3D structures|Chitinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chitinase]] | + | [[Category: Hevea brasiliensis]] |
| - | [[Category: Hevbr]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hermoso, J A]] | + | [[Category: Hermoso JA]] |
| - | [[Category: Martinez-Caballero, S]] | + | [[Category: Martinez-Caballero S]] |
| - | [[Category: Rodriguez-Romero, A]] | + | [[Category: Rodriguez-Romero A]] |
| - | [[Category: All alpha]]
| + | |
| - | [[Category: Chitinase-like protein]]
| + | |
| - | [[Category: Extracellular]]
| + | |
| - | [[Category: Hydrolase-like protein]]
| + | |
| - | [[Category: Inactive chitinase]]
| + | |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
CHI1_HEVBR Inactive chitinase-like protein that does not exhibit hydrolytic activity toward chitin (PubMed:25104038). Binds strongly to chitin and possesses antifungal activity toward the fungal pathogen Altenaria alternata in plate assays (PubMed:25104038). Inhibits the growth of Fusarium oxysporum on plate assays (PubMed:11940078). Probably involved in defense against fungal pathogens through a mechanism that only involves carbohydrate binding (PubMed:25104038).[1] [2]
Publication Abstract from PubMed
Plants express chitinase and chitinase-like proteins (CLP) belonging to the glycosyl hydrolases of the GH18 and GH19 families, which exhibit varied functions. CLPs in the GH18 family have been structurally and functionally characterized; however, there are no structures available for any member of the GH19 family. In this study, two CLPs of the GH19 family from the rubber tree Hevea brasiliensis (HbCLP1 and HbCLP2) were cloned, expressed, and characterized. HbCLP1 was identical to the allergen Hev b 11.0101 previously described by others, while HbCLP2 was a novel isoform exhibiting an unusual half chitin-binding domain before the catalytic domain (CatD). Sequence alignments showed that in both proteins, the catalytic residues Glu117 and Glu147 in HbCLP1 and HbCLP2, respectively, were mutated to Ala, accounting for the lack of activity. Nonetheless, both CLPs bound chitin and chitotriose (GlcNAc)3 with high affinities, as evaluated with chitin-affinity chromatography and tryptophan fluorescence experiments. The chitin binding domains (CBD) also bound chitotriose with even higher affinities. The crystal structures of the HbCLP1-isolated domains were determined at high resolution. The analysis of the crystallographic models and docking experiments using (GlcNAc)6 oligosaccharides provide evidence of the residues involved in sugar binding. Endochitinase activity was restored in both proteins by mutating residues A117E (HbCLP1) and A147E (HbCLP2); the distance between the catalytic proton donor and the catalytic nucleophile in the in silico mutated residues was 9.5 A, as occurs in inverting enzymes. HbCLP1 and HbCLP2 were highly thermostable and exhibited antifungal activity against Alternaria alternate, suggesting their participation in plant defense mechanisms. This article is protected by copyright. All rights reserved.
Comparative study of two GH19 chitinase-like proteins from Hevea brasiliensis, one exhibiting a novel carbohydrate-binding domain.,Martinez-Caballero S, Cano-Sanchez P, Mares-Mejia I, Diaz-Sanchez AG, Macias-Rubalcava ML, Hermoso JA, Rodriguez-Romero A FEBS J. 2014 Aug 8. doi: 10.1111/febs.12962. PMID:25104038[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ O'Riordain G, Radauer C, Hoffmann-Sommergruber K, Adhami F, Peterbauer CK, Blanco C, Godnic-Cvar J, Scheiner O, Ebner C, Breiteneder H. Cloning and molecular characterization of the Hevea brasiliensis allergen Hev b 11, a class I chitinase. Clin Exp Allergy. 2002 Mar;32(3):455-62. doi: 10.1046/j.1365-2222.2002.01312.x. PMID:11940078 doi:http://dx.doi.org/10.1046/j.1365-2222.2002.01312.x
- ↑ Martinez-Caballero S, Cano-Sanchez P, Mares-Mejia I, Diaz-Sanchez AG, Macias-Rubalcava ML, Hermoso JA, Rodriguez-Romero A. Comparative study of two GH19 chitinase-like proteins from Hevea brasiliensis, one exhibiting a novel carbohydrate-binding domain. FEBS J. 2014 Aug 8. doi: 10.1111/febs.12962. PMID:25104038 doi:http://dx.doi.org/10.1111/febs.12962
- ↑ Martinez-Caballero S, Cano-Sanchez P, Mares-Mejia I, Diaz-Sanchez AG, Macias-Rubalcava ML, Hermoso JA, Rodriguez-Romero A. Comparative study of two GH19 chitinase-like proteins from Hevea brasiliensis, one exhibiting a novel carbohydrate-binding domain. FEBS J. 2014 Aug 8. doi: 10.1111/febs.12962. PMID:25104038 doi:http://dx.doi.org/10.1111/febs.12962
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