View source for 5zns


==Insect chitin deacetylase==
<StructureSection load='5zns' size='340' side='right'caption='[[5zns]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zns]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZNS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.396&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5zns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zns OCA], [https://pdbe.org/5zns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zns RCSB], [https://www.ebi.ac.uk/pdbsum/5zns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zns ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CDA1_BOMMO CDA1_BOMMO] Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin.<ref>PMID:30755482</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Insect chitin deacetylases (CDAs) catalyze the removal of acetyl groups from chitin and modify this polymer during its synthesis and reorganization. CDAs are essential for insect survival and therefore represent promising targets for insecticide development. However, the structural and biochemical characteristics of insect CDAs have remained elusive. Here, we report the crystal structures of two insect CDAs from the silkmoth Bombyx mori: BmCDA1, which may function in cuticle modification, and BmCDA8, which may act in modifying peritrophic membranes in the midgut. Both enzymes belong to the carbohydrate esterase 4 (CE4) family. Comparing their overall structures at 1.98-2.4 A resolution with those from well-studied microbial CDAs, we found that two unique loop regions in BmCDA1 and BmCDA8 contribute to the distinct architecture of their substrate-binding clefts. These comparisons revealed that both BmCDA1 and BmCDA8 possess a much longer and wider substrate-binding cleft with a very open active site in the center than the microbial CDAs including VcCDA from Vibrio cholerae and ArCE4A from Arthrobacter species AW19M34-1. Biochemical analyses indicated that BmCDA8 is an active enzyme that requires its substrates to occupy subsites 0, +1, and +2 for catalysis. In contrast, BmCDA1 also required accessory proteins for catalysis. To the best of our knowledge, our work is the first to unveil the structural and biochemical features of insect proteins belonging to the CE4 family.

Structural and biochemical insights into the catalytic mechanisms of two insect chitin deacetylases of the carbohydrate esterase 4 family.,Liu L, Zhou Y, Qu M, Qiu Y, Guo X, Zhang Y, Liu T, Yang J, Yang Q J Biol Chem. 2019 Feb 12. pii: RA119.007597. doi: 10.1074/jbc.RA119.007597. PMID:30755482<ref>PMID:30755482</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zns" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bombyx mori]]
[[Category: Large Structures]]
[[Category: Liu L]]
[[Category: Yang Q]]
[[Category: Zhou Y]]