4mck: Difference between revisions

Latest revision as of 11:09, 6 November 2024

Crystal structure of Family GH19, Class IV chitinase from Zea mays

Structural highlights

4mck is a 1 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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:https://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:https://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:https://dx.doi.org/10.1002/pro.2437

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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

[4] 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

[5] 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:https://dx.doi.org/10.1111/all.13164

[6] 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

[7] 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

[8] 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:https://dx.doi.org/10.1002/pro.2437

[9] 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:https://dx.doi.org/10.1002/pro.2437

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@@ Line 1: / Line 1: @@
 ==Crystal structure of Family GH19, Class IV chitinase from Zea mays==
-<StructureSection load='4mck' size='340' side='right' caption='[[4mck]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+<StructureSection load='4mck' size='340' side='right'caption='[[4mck]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == 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 id='NonStdRes'><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]] 1.5&#8491;</td></tr>
-<tr id='related'><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 id='gene'><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>
-<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=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>
 </table>
+== Function ==
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4mck" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Chitinase 3D structures|Chitinase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </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]]

4mck: Difference between revisions

Latest revision as of 11:09, 6 November 2024

Crystal structure of Family GH19, Class IV chitinase from Zea mays

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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