4d3w: Difference between revisions
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<StructureSection load='4d3w' size='340' side='right'caption='[[4d3w]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='4d3w' size='340' side='right'caption='[[4d3w]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4d3w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4d3w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_glabrata_CBS_138 Candida glabrata CBS 138]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D3W FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</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=4d3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3w OCA], [https://pdbe.org/4d3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d3w RCSB], [https://www.ebi.ac.uk/pdbsum/4d3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d3w ProSAT]</span></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=4d3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3w OCA], [https://pdbe.org/4d3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d3w RCSB], [https://www.ebi.ac.uk/pdbsum/4d3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d3w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q6FUW5_CANGA Q6FUW5_CANGA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 15:20, 20 December 2023
Crystal Structure of Epithelial Adhesin 1 A domain (Epa1A) from Candida glabrata in complex with the T-antigen (Galb1-3GalNAc)Crystal Structure of Epithelial Adhesin 1 A domain (Epa1A) from Candida glabrata in complex with the T-antigen (Galb1-3GalNAc)
Structural highlights
FunctionPublication Abstract from PubMedFor host colonization, the human fungal pathogen Candida glabrata is known to utilize a large family of highly related surface-exposed cell wall proteins, the lectin-like epithelial adhesins (Epas). To reveal the structure-function relationships within the entire Epa family, we have performed a large-scale functional analysis of the adhesion (A) domains of seventeen Epa paralogs in combination with 3D-structural studies of selected members with cognate ligands. Our study shows that most EpaA domains exert lectin-like functions and together recognize a wide variety of glycans with terminal galactosides for conferring epithelial cell adhesion. We further identify several conserved and variable structural features within the diverse Epa ligand binding pockets, which affect affinity and specificity. These features rationalize why mere phylogenetic relationships within the Epa family are weak indicators for functional classification and explain how Epa-like adhesins have evolved in C. glabrata and related fungal species. Structural Hotspots Determine Functional Diversity of the Candida glabrata Epithelial Adhesin Family.,Diderrich R, Kock M, Maestre-Reyna M, Keller P, Steuber H, Rupp S, Essen LO, Mosch HU J Biol Chem. 2015 Jun 23. pii: jbc.M115.655654. PMID:26105055[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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