4afa

Crystal Structure of subtype-switched Epithelial Adhesin 1 to 2 A domain (Epa1to2A) from Candida glabrata in complex with glycerol

spinqualitylabelsall models 4afa, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4afa is a 1 chain structure with sequence from Candida glabrata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: CA, GAL, GLC, GOL, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6VBJ0_CANGB Publication Abstract from PubMed The human pathogenic yeast Candida glabrata harbors more than 20 surface-exposed, epithelial adhesins (Epas) for host cell adhesion. The Epa family recognizes host glycans and discriminates between target tissues by their adhesin (A) domains, but a detailed structural basis for ligand-binding specificity of Epa proteins has been lacking so far. In this study, we provide high-resolution crystal structures of the Epa1A domain in complex with different carbohydrate ligands that reveal how host cell mucin-type O-glycans are recognized and allow a structure-guided classification of the Epa family into specific subtypes. Further detailed structural and functional characterization of subtype-switched Epa1 variants shows that specificity is governed by two inner loops, CBL1 and CBL2, involved in calcium binding as well as by three outer loops, L1, L2, and L3. In summary, our study provides the structural basis for promiscuity and specificity of Epa adhesins, which might further contribute to developing anti-adhesive antimycotics and combating Candida colonization. Structural basis for promiscuity and specificity during Candida glabrata invasion of host epithelia.,Maestre-Reyna M, Diderrich R, Veelders MS, Eulenburg G, Kalugin V, Bruckner S, Keller P, Rupp S, Mosch HU, Essen LO Proc Natl Acad Sci U S A. 2012 Oct 3. PMID:23035251 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adhesin 3D structures

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