7stn: Difference between revisions

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New page: '''Unreleased structure''' The entry 7stn is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 7stn is ON HOLD  until Paper Publication
==Chitin Synthase 2 from Candida albicans bound to Nikkomycin Z==
<StructureSection load='7stn' size='340' side='right'caption='[[7stn]], [[Resolution|resolution]] 3.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7stn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7STN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7STN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.19&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>3PE</scene>, <scene name='pdbligand=BGI:(2S)-{[(2S,3S,4S)-2-amino-4-hydroxy-4-(5-hydroxypyridin-2-yl)-3-methylbutanoyl]amino}[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxyoxolan-2-yl]acetic+acid+(non-preferred+name)'>BGI</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=7stn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7stn OCA], [https://pdbe.org/7stn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7stn RCSB], [https://www.ebi.ac.uk/pdbsum/7stn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7stn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CHS2_CANAX CHS2_CANAX] Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Chitin is an essential component of the fungal cell wall. Chitin synthases (Chss) catalyze chitin formation and translocation across the membrane and are targets of antifungal agents, including nikkomycin Z and polyoxin D. Lack of structural insights into the action of these inhibitors on Chs has hampered their further development to the clinic. We present the cryo-EM structures of Chs2 from Candida albicans (CaChs2) in the apo, substrate-bound, nikkomycin Z-bound, and polyoxin D-bound states. CaChs2 adopts a unique domain-swapped dimer configuration where a conserved motif in the domain-swapped region controls enzyme activity. CaChs2 has a dual regulation mechanism where the chitin translocation tunnel is closed by the extracellular gate and plugged by a lipid molecule in the apo state to prevent non-specific leak. Analyses of substrate and inhibitor binding provide insights into the chemical logic of Chs inhibition, which can guide Chs-targeted antifungal development.


Authors:  
Structural basis for inhibition and regulation of a chitin synthase from Candida albicans.,Ren Z, Chhetri A, Guan Z, Suo Y, Yokoyama K, Lee SY Nat Struct Mol Biol. 2022 Jul;29(7):653-664. doi: 10.1038/s41594-022-00791-x. , Epub 2022 Jul 4. PMID:35788183<ref>PMID:35788183</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7stn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Candida albicans]]
[[Category: Large Structures]]
[[Category: Chhetri A]]
[[Category: Lee S]]
[[Category: Ren Z]]
[[Category: Yokoyama K]]

Latest revision as of 05:53, 5 June 2024

Chitin Synthase 2 from Candida albicans bound to Nikkomycin Z

7stn, resolution 3.19Å

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