4mck

From Proteopedia

(Difference between revisions)

Current revision

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: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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4mck"

Categories: Large Structures | Zea mays | Chaudet MM | Rose DR

@@ 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

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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