5z34

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==The structure of a chitin deacetylase from Bombyx mori provide the first insight into insect chitin deacetylation mechanism==
==The structure of a chitin deacetylase from Bombyx mori provide the first insight into insect chitin deacetylation mechanism==
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<StructureSection load='5z34' size='340' side='right' caption='[[5z34]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='5z34' size='340' side='right'caption='[[5z34]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5z34]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z34 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z34 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5z34]] 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=5Z34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z34 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.399&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitin_deacetylase Chitin deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.41 3.5.1.41] </span></td></tr>
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<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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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=5z34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z34 OCA], [http://pdbe.org/5z34 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z34 RCSB], [http://www.ebi.ac.uk/pdbsum/5z34 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z34 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5z34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z34 OCA], [https://pdbe.org/5z34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z34 RCSB], [https://www.ebi.ac.uk/pdbsum/5z34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z34 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The ectoperitrophic space (EcPS) between the insect midgut epithelial cells and the peritrophic matrix is an unexplored, clean resource for concentrated proteins secreted by the midgut epithelial cells, which offers an ideal opportunity to uncover the midgut functions. In this study, we used Bombyx mori as a model organism and performed comparative proteomic analyses of the secreted proteins in the EcPS at the feeding and wandering stages. A total of 372 proteins were identified from both stages and 70 proteins were predicted to be secreted. Amongst these proteins, 17 secreted digestive proteins were identified and their temporal and spatial transcriptional expression patterns demonstrated that all these proteins were up-regulated at the feeding stage and differentially expressed in different parts of the midgut. Proteins with nutrient reservoir activity and defence activity were found to be up-regulated at the wandering stage. This work is the first to show the presence of digestive enzymes in the EcPS of the insect midgut using a proteomic approach, which provides evidence that suggests a physiological functional differentiation of the insect midgut. It is very clear that the EcPS undergoes dynamic changes in its composition of proteins in response to the changing needs of the insect at different developmental stages.
 
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The physiological differentiation along the midgut of Bombyx mori - inspirations from proteomics and gene expression patterns of the secreted proteins in the ectoperitrophic space.,Liu L, Qu M, Yang J, Yang Q Insect Mol Biol. 2018 Apr;27(2):247-259. doi: 10.1111/imb.12368. Epub 2017 Dec, 18. PMID:29251378<ref>PMID:29251378</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 5z34" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chitin deacetylase]]
 
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[[Category: Liu, L]]
 
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[[Category: Yang, Q]]
 
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[[Category: Zhou, Y]]
 
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[[Category: Activity]]
 
[[Category: Bombyx mori]]
[[Category: Bombyx mori]]
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[[Category: Chitin binding]]
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[[Category: Large Structures]]
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[[Category: Hydrolase]]
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[[Category: Liu L]]
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[[Category: Yang Q]]
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[[Category: Zhou Y]]

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The structure of a chitin deacetylase from Bombyx mori provide the first insight into insect chitin deacetylation mechanism

PDB ID 5z34

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