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| <StructureSection load='7o9p' size='340' side='right'caption='[[7o9p]], [[Resolution|resolution]] 1.99Å' scene=''> | | <StructureSection load='7o9p' size='340' side='right'caption='[[7o9p]], [[Resolution|resolution]] 1.99Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7o9p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O9P FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O9P FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GD:GADOLINIUM+ATOM'>GD</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]] 1.99Å</td></tr> |
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GD:GADOLINIUM+ATOM'>GD</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=7o9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o9p OCA], [https://pdbe.org/7o9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o9p RCSB], [https://www.ebi.ac.uk/pdbsum/7o9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o9p 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=7o9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o9p OCA], [https://pdbe.org/7o9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o9p RCSB], [https://www.ebi.ac.uk/pdbsum/7o9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o9p ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| Candida glabrata is an opportunistic pathogenic yeast frequently causing infections in humans. Though it lacks typical virulence factors such as hyphal development, C. glabrata contains a remarkably large and diverse set of putative wall adhesins that is crucial for its success as pathogen. Here, we present an analysis of putative adhesins from the homology clusters V and VI. First, sequence similarity network analysis revealed relationships between cluster V and VI adhesins and S. cerevisiae haze protective factors (Hpf). Crystal structures of A-regions from cluster VI adhesins Awp1 and Awp3b reveal a parallel right-handed beta-helix domain that is linked to a C-terminal beta-sandwich. Structure solution of the A-region of Awp3b via single wavelength anomalous diffraction phasing revealed the largest known lanthanide cluster with 21 Gd3+ ions. Awp1-A and Awp3b-A show structural similarity to pectate lyases but binding to neither carbohydrates nor Ca2+ was observed. Phenotypic analysis of awp1Delta, awp3Delta, and awp1,3Delta double mutants did also not confirm their role as adhesins. In contrast, deletion mutants of the cluster V adhesin Awp2 in the hyperadhesive clinical isolate PEU382 demonstrated its importance for adhesion to polystyrene or glass, biofilm formation, cell aggregation and other cell surface-related phenotypes. Together with cluster III and VII adhesins our study shows that C. glabrata CBS138 can rely on a set of 42 Awp1-related adhesins with beta-helix/alpha-crystallin domain architecture for modifying the surface characteristics of its cell wall.
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| A novel class of Candida glabrata cell wall proteins with beta-helix fold mediates adhesion in clinical isolates.,Reithofer V, Fernandez-Pereira J, Alvarado M, de Groot P, Essen LO PLoS Pathog. 2021 Dec 28;17(12):e1009980. doi: 10.1371/journal.ppat.1009980., eCollection 2021 Dec. PMID:34962966<ref>PMID:34962966</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7o9p" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Essen, L O]] | | [[Category: Essen L-O]] |
| [[Category: Groot, P de]]
| | [[Category: Reithofer V]] |
| [[Category: Reithofer, V]] | | [[Category: De Groot P]] |
| [[Category: Adhesin]] | |
| [[Category: Adhesin-like wall protein]]
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| [[Category: Adhesion]]
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| [[Category: Awp]]
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| [[Category: Beta-helix]]
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| [[Category: Candida glabrata]]
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| [[Category: Cell adhesion]]
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| [[Category: Gadolinium]]
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| [[Category: Gadolinium cluster]]
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| [[Category: Haze-protective factor]]
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| [[Category: Lanthanide]]
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| [[Category: Lanthanide cluster]]
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