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PDBsum entry 4afc
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Cell adhesion
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PDB id
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4afc
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PDB id:
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| Name: |
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Cell adhesion
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Title:
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Crystal structure of subtype-switched epithelial adhesin 1 to 6 a domain (epa1to6a) from candida glabrata in complex with galb1-3glc
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Structure:
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Epa1p. Chain: a. Fragment: adhesion domain (a domain), residues 31-271. Synonym: epithelial adhesin 1. Engineered: yes. Mutation: yes. Other_details: sub-type switched epa1a variant which emulates the binding pocket of epa6a
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Source:
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Candida glabrata. Organism_taxid: 5478. Strain: cbs138. Atcc: 2001. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.55Å
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R-factor:
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0.145
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R-free:
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0.171
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Authors:
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M.Maestre-Reyna,R.Diderrich,M.S.Veelders,G.Eulenburg,V.Kalugin, S.Brueckner,P.Keller,S.Rupp,H.-U.Moesch,L.-O.Essen
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Key ref:
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M.Maestre-Reyna
et al.
(2012).
Structural basis for promiscuity and specificity during Candida glabrata invasion of host epithelia.
Proc Natl Acad Sci U S A,
109,
16864-16869.
PubMed id:
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Date:
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18-Jan-12
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Release date:
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17-Oct-12
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PROCHECK
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Headers
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References
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Q6VBJ0
(Q6VBJ0_CANGB) -
Epa1p from Candida glabrata
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Seq:
Struc:
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1034 a.a.
229 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Proc Natl Acad Sci U S A
109:16864-16869
(2012)
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PubMed id:
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Structural basis for promiscuity and specificity during Candida glabrata invasion of host epithelia.
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M.Maestre-Reyna,
R.Diderrich,
M.S.Veelders,
G.Eulenburg,
V.Kalugin,
S.Brückner,
P.Keller,
S.Rupp,
H.U.Mösch,
L.O.Essen.
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ABSTRACT
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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.
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Links
