6jm8: Difference between revisions
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<StructureSection load='6jm8' size='340' side='right'caption='[[6jm8]], [[Resolution|resolution]] 1.91Å' scene=''> | <StructureSection load='6jm8' size='340' side='right'caption='[[6jm8]], [[Resolution|resolution]] 1.91Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6jm8]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6jm8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ostrinia_furnacalis Ostrinia furnacalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JM8 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 1.911Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=6jm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jm8 OCA], [https://pdbe.org/6jm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jm8 RCSB], [https://www.ebi.ac.uk/pdbsum/6jm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jm8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A482LWB1_OSTFU A0A482LWB1_OSTFU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The antifungal activity of insect chitinase has rarely been studied. Here, we show that chitinase ChtIV, which is specifically expressed in the midgut of Asian corn borer (Ostrinia furnacalis), has antifungal activity toward phytopathogenic fungi. ChtIV exhibited high stability and mycelial hydrolytic activity in the extreme midgut environment, which has a pH of 10 and is rich in proteases. Hyper-N-glycosylation and reduced electrostatic interactions ensure the stability of ChtIV in the midgut. The structural characteristics of ChtIV are similar to two plant antifungal chitinases but distinct from an insect chitinase for cuticular chitin degradation in both the substrate-binding cleft and auxiliary binding motif. Since the phytopathogenic fungi are those that frequently invade corn, ChtIV may play a role in insect immune system and become a potential pesticide target. The crystal structures of ChtIV and its complexes with penta-N-acetylchitopentaose (a substrate) and allosamidin (an inhibitor) were obtained, which may facilitate rational design of ChtIV inhibitors as agrichemicals. | |||
Structural and biochemical insights into an insect gut-specific chitinase with antifungal activity.,Liu T, Guo X, Bu Y, Zhou Y, Duan Y, Yang Q Insect Biochem Mol Biol. 2020 Apr;119:103326. doi: 10.1016/j.ibmb.2020.103326. , Epub 2020 Jan 20. PMID:31968227<ref>PMID:31968227</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6jm8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Chitinase 3D structures|Chitinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ostrinia furnacalis]] | ||
[[Category: | [[Category: Liu T]] | ||
[[Category: | [[Category: Yang Q]] | ||
Latest revision as of 13:15, 22 November 2023
Crystal structure of Ostrinia furnacalis Group IV chitinaseCrystal structure of Ostrinia furnacalis Group IV chitinase
Structural highlights
FunctionPublication Abstract from PubMedThe antifungal activity of insect chitinase has rarely been studied. Here, we show that chitinase ChtIV, which is specifically expressed in the midgut of Asian corn borer (Ostrinia furnacalis), has antifungal activity toward phytopathogenic fungi. ChtIV exhibited high stability and mycelial hydrolytic activity in the extreme midgut environment, which has a pH of 10 and is rich in proteases. Hyper-N-glycosylation and reduced electrostatic interactions ensure the stability of ChtIV in the midgut. The structural characteristics of ChtIV are similar to two plant antifungal chitinases but distinct from an insect chitinase for cuticular chitin degradation in both the substrate-binding cleft and auxiliary binding motif. Since the phytopathogenic fungi are those that frequently invade corn, ChtIV may play a role in insect immune system and become a potential pesticide target. The crystal structures of ChtIV and its complexes with penta-N-acetylchitopentaose (a substrate) and allosamidin (an inhibitor) were obtained, which may facilitate rational design of ChtIV inhibitors as agrichemicals. Structural and biochemical insights into an insect gut-specific chitinase with antifungal activity.,Liu T, Guo X, Bu Y, Zhou Y, Duan Y, Yang Q Insect Biochem Mol Biol. 2020 Apr;119:103326. doi: 10.1016/j.ibmb.2020.103326. , Epub 2020 Jan 20. PMID:31968227[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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