6bt9: Difference between revisions
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<StructureSection load='6bt9' size='340' side='right'caption='[[6bt9]], [[Resolution|resolution]] 2.26Å' scene=''> | <StructureSection load='6bt9' size='340' side='right'caption='[[6bt9]], [[Resolution|resolution]] 2.26Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6bt9]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6bt9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BT9 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6bt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bt9 OCA], [https://pdbe.org/6bt9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bt9 RCSB], [https://www.ebi.ac.uk/pdbsum/6bt9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bt9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A243G6Q6_BACTU A0A243G6Q6_BACTU] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus | [[Category: Bacillus thuringiensis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Barboza-Corona | [[Category: Barboza-Corona J]] | ||
[[Category: Brieba | [[Category: Brieba LG]] | ||
[[Category: Jimenez-Sandoval | [[Category: Jimenez-Sandoval P]] | ||
[[Category: Juarez-Hernandez | [[Category: Juarez-Hernandez E]] | ||
[[Category: Torres-Larios | [[Category: Torres-Larios A]] | ||
Revision as of 17:49, 4 October 2023
Chitinase ChiA74 from Bacillus thuringiensisChitinase ChiA74 from Bacillus thuringiensis
Structural highlights
FunctionPublication Abstract from PubMedThere is no structural information about any chitinase synthesized by Bacillus thuringiensis, the most successful microbial insect larvicide used worldwide. In this study, we solved the 3D structure of the chitinase ChiA74 at 2.26 A. The crystal structure shows that ChiA74 is composed of a modular arrangement formed by (i) a catalytic region (CD), (ii) a chitinase insertion domain (CID), (iii) a fibronectin type III domain (FnIII), and (iv) a chitin binding domain (CBD). The location of the CBD with respect to the CD has no structural similarity to other chitinases with known structures. The activity of a ChiA74 lacking its secretion signal peptide (ChiA74Deltasp) and a truncated version lacking its CBD/FnIII domains (ChiA74Deltasp-50) did not have statistical differences in activity against colloidal chitin. However, ChiA74Deltasp exhibits 4.5 and 2.0 higher activity than versions lacking the CBD (ChiA74Deltasp-60) and CBD/FnIII domains (ChiA74Deltasp-50), respectively, when crystalline chitin was used as substrate. Our data suggest that the CBD might plays a significant role in crystalline chitin hydrolysis. We also demonstrated the importance of the catalytic E211 in the CD, as mutants ChiA74DeltaspE211N and ChiA74DeltaspD207N, E211N were inactive against colloidal and crystalline chitins, chitosan and 4-MU-GlcNAc3. ChiA74 has a processive activity producing oligosaccharides with degree of polymerization (DP) of 1 (GlcNAc) and 2 (GlcNAc2). The crystal structure of the chitinase ChiA74 of Bacillus thuringiensis has a multidomain assembly.,Juarez-Hernandez EO, Casados-Vazquez LE, Brieba LG, Torres-Larios A, Jimenez-Sandoval P, Barboza-Corona JE Sci Rep. 2019 Feb 22;9(1):2591. doi: 10.1038/s41598-019-39464-z. PMID:30796308[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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