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==Crystal Structure of Epithelial Adhesin 6 A domain (Epa6A) from Candida glabrata in complex with Gala1-3Gal== | ==Crystal Structure of Epithelial Adhesin 6 A domain (Epa6A) from Candida glabrata in complex with Gala1-3Gal== | ||
<StructureSection load='4cov' size='340' side='right' caption='[[4cov]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='4cov' size='340' side='right'caption='[[4cov]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4cov]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4COV OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4cov]] 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=4COV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4COV FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene> | </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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cov OCA], [https://pdbe.org/4cov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cov RCSB], [https://www.ebi.ac.uk/pdbsum/4cov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cov ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6FX55_CANGA Q6FX55_CANGA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
For 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<ref>PMID:26105055</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4cov" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Adhesin 3D structures|Adhesin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Diderrich | [[Category: Large Structures]] | ||
[[Category: Essen | [[Category: Diderrich R]] | ||
[[Category: Kock | [[Category: Essen L-O]] | ||
[[Category: Maestre-Reyna | [[Category: Kock M]] | ||
[[Category: Moesch | [[Category: Maestre-Reyna M]] | ||
[[Category: Moesch H-U]] | |||
Latest revision as of 15:14, 20 December 2023
Crystal Structure of Epithelial Adhesin 6 A domain (Epa6A) from Candida glabrata in complex with Gala1-3GalCrystal Structure of Epithelial Adhesin 6 A domain (Epa6A) from Candida glabrata in complex with Gala1-3Gal
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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