7stl: Difference between revisions
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==Chitin Synthase 2 from Candida albicans at the apo state== | ==Chitin Synthase 2 from Candida albicans at the apo state== | ||
<StructureSection load='7stl' size='340' side='right'caption='[[7stl]]' scene=''> | <StructureSection load='7stl' size='340' side='right'caption='[[7stl]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7STL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7STL FirstGlance]. <br> | <table><tr><td colspan='2'>[[7stl]] 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=7STL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7STL FirstGlance]. <br> | ||
</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=7stl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7stl OCA], [https://pdbe.org/7stl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7stl RCSB], [https://www.ebi.ac.uk/pdbsum/7stl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7stl ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.95Å</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></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=7stl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7stl OCA], [https://pdbe.org/7stl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7stl RCSB], [https://www.ebi.ac.uk/pdbsum/7stl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7stl ProSAT]</span></td></tr> | |||
</table> | </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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7stl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Candida albicans]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chhetri A]] | [[Category: Chhetri A]] | ||
Latest revision as of 08:53, 5 June 2024
Chitin Synthase 2 from Candida albicans at the apo stateChitin Synthase 2 from Candida albicans at the apo state
Structural highlights
FunctionCHS2_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. Publication Abstract from PubMedChitin 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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