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| | ==Crystal structure of Family GH19, Class IV chitinase from Zea mays== | | ==Crystal structure of Family GH19, Class IV chitinase from Zea mays== |
| - | <StructureSection load='4mck' size='340' side='right' caption='[[4mck]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='4mck' size='340' side='right'caption='[[4mck]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4mck]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Maize Maize]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MCK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4mck]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MCK FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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]] 1.5Å</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mcl|4mcl]]</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=4mck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mck OCA], [https://pdbe.org/4mck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mck RCSB], [https://www.ebi.ac.uk/pdbsum/4mck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mck ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">chiA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4577 MAIZE])</td></tr>
| + | </table> |
| - | <tr><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> | + | == Function == |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mck OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mck RCSB], [http://www.ebi.ac.uk/pdbsum/4mck PDBsum]</span></td></tr>
| + | [https://www.uniprot.org/uniprot/CHIA_MAIZE CHIA_MAIZE] Defense against chitin-containing fungal pathogens (PubMed:1551872, Ref.6). Hydrolyzes glycol chitin and tetra-N-acetylchitotetraose in vitro (PubMed:28328103). Its action is countered by fungal polyglycine hydrolases and fungalysin, that cleave the chitin-binding domain from the protein (PubMed:21453431, PubMed:24627966, PubMed:25966977, PubMed:35240278, PubMed:36762862, Ref.6).<ref>PMID:1551872</ref> <ref>PMID:21453431</ref> <ref>PMID:24627966</ref> <ref>PMID:25966977</ref> <ref>PMID:28328103</ref> <ref>PMID:35240278</ref> <ref>PMID:36762862</ref> <ref>PMID:24616181</ref> |
| - | <table> | + | |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | Crystallographic structure of ChitA, a glycoside hydrolase family 19, plant class IV chitinase from Zea mays.,Chaudet MM, Naumann TA, Price NP, Rose DR Protein Sci. 2014 Feb 6. doi: 10.1002/pro.2437. PMID:24616181<ref>PMID:24616181</ref> | | Crystallographic structure of ChitA, a glycoside hydrolase family 19, plant class IV chitinase from Zea mays.,Chaudet MM, Naumann TA, Price NP, Rose DR Protein Sci. 2014 Feb 6. doi: 10.1002/pro.2437. PMID:24616181<ref>PMID:24616181</ref> |
| | | | |
| - | 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 4mck" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Chitinase 3D structures|Chitinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chitinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Maize]] | + | [[Category: Zea mays]] |
| - | [[Category: Chaudet, M M.]] | + | [[Category: Chaudet MM]] |
| - | [[Category: Rose, D R.]] | + | [[Category: Rose DR]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
CHIA_MAIZE Defense against chitin-containing fungal pathogens (PubMed:1551872, Ref.6). Hydrolyzes glycol chitin and tetra-N-acetylchitotetraose in vitro (PubMed:28328103). Its action is countered by fungal polyglycine hydrolases and fungalysin, that cleave the chitin-binding domain from the protein (PubMed:21453431, PubMed:24627966, PubMed:25966977, PubMed:35240278, PubMed:36762862, Ref.6).[1] [2] [3] [4] [5] [6] [7] [8]
Publication Abstract from PubMed
Maize ChitA chitinase is composed of a small, hevein-like domain attached to a carboxy-terminal chitinase domain. During fungal ear rot, the hevein-like domain is cleaved by secreted fungal proteases to produce truncated forms of ChitA. Here, we report a structural and biochemical characterization of truncated ChitA (ChitA DeltaN), which lacks the hevein-like domain. ChitA DeltaN and a mutant form (ChitA DeltaN-EQ) were expressed and purified; enzyme assays showed that ChitA DeltaN activity was comparable to the full-length enzyme. Mutation of Glu62 to Gln (ChitA DeltaN-EQ) abolished chitinase activity without disrupting substrate binding, demonstrating that Glu62 is directly involved in catalysis. A crystal structure of ChitA DeltaN-EQ provided strong support for key roles for Glu62, Arg177, and Glu165 in hydrolysis, and for Ser103 and Tyr106 in substrate binding. These findings demonstrate that the hevein-like domain is not needed for enzyme activity. Moreover, comparison of the crystal structure of this plant class IV chitinase with structures from larger class I and II enzymes suggest that class IV chitinases have evolved to accommodate shorter substrates.
Crystallographic structure of ChitA, a glycoside hydrolase family 19, plant class IV chitinase from Zea mays.,Chaudet MM, Naumann TA, Price NP, Rose DR Protein Sci. 2014 Feb 6. doi: 10.1002/pro.2437. PMID:24616181[9]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Huynh QK, Hironaka CM, Levine EB, Smith CE, Borgmeyer JR, Shah DM. Antifungal proteins from plants. Purification, molecular cloning, and antifungal properties of chitinases from maize seed. J Biol Chem. 1992 Apr 5;267(10):6635-40. PMID:1551872
- ↑ Naumann TA. Modification of recombinant maize ChitA chitinase by fungal chitinase-modifying proteins. Mol Plant Pathol. 2011 May;12(4):365-72. PMID:21453431 doi:10.1111/j.1364-3703.2010.00677.x
- ↑ Naumann TA, Wicklow DT, Price NP. Polyglycine hydrolases secreted by Pleosporineae fungi that target the linker region of plant class IV chitinases. Biochem J. 2014 Jun 1;460(2):187-98. PMID:24627966 doi:10.1042/BJ20140268
- ↑ Naumann TA, Naldrett MJ, Ward TJ, Price NP. Polyglycine hydrolases: Fungal β-lactamase-like endoproteases that cleave polyglycine regions within plant class IV chitinases. Protein Sci. 2015 Jul;24(7):1147-57. PMID:25966977 doi:10.1002/pro.2705
- ↑ Volpicella M, Leoni C, Fanizza I, Distaso M, Leoni G, Farioli L, Naumann T, Pastorello E, Ceci LR. Characterization of maize chitinase-A, a tough allergenic molecule. Allergy. 2017 Sep;72(9):1423-1429. doi: 10.1111/all.13164. Epub 2017 May 11. PMID:28328103 doi:http://dx.doi.org/10.1111/all.13164
- ↑ Naumann TA, Sollenberger KG, Hao G. Production of selenomethionine labeled polyglycine hydrolases in Pichia pastoris. Protein Expr Purif. 2022 Jun;194:106076. PMID:35240278 doi:10.1016/j.pep.2022.106076
- ↑ Dowling NV, Naumann TA, Price NPJ, Rose DR. Crystal structure of a polyglycine hydrolase determined using a RoseTTAFold model. Acta Crystallogr D Struct Biol. 2023 Feb 1;79(Pt 2):168-176. PMID:36762862 doi:10.1107/S2059798323000311
- ↑ Chaudet MM, Naumann TA, Price NP, Rose DR. Crystallographic structure of ChitA, a glycoside hydrolase family 19, plant class IV chitinase from Zea mays. Protein Sci. 2014 Feb 6. doi: 10.1002/pro.2437. PMID:24616181 doi:http://dx.doi.org/10.1002/pro.2437
- ↑ Chaudet MM, Naumann TA, Price NP, Rose DR. Crystallographic structure of ChitA, a glycoside hydrolase family 19, plant class IV chitinase from Zea mays. Protein Sci. 2014 Feb 6. doi: 10.1002/pro.2437. PMID:24616181 doi:http://dx.doi.org/10.1002/pro.2437
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