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@ARTICLE{Mesarich:139940,
author = {Mesarich, Carl H. and Schmitz, Michael and Tremouilhac,
Pierre and McGillivray, Duncan J. and Templeton, Matthew D.
and Dingley, Andrew},
title = {{S}tructure, dynamics and domain organization of the repeat
protein {C}in1 from the apple scab fungus},
journal = {Biochimica et biophysica acta / Proteins and proteomics},
volume = {1824},
number = {10},
issn = {1570-9639},
address = {Amsterdam [u.a.]},
publisher = {Elsevier},
reportid = {FZJ-2013-05907},
pages = {1118 - 1128},
year = {2012},
abstract = {Venturia inaequalis is a hemi-biotrophic fungus that causes
scab disease of apple. A recently-identified gene from this
fungus, cin1 (cellophane-induced 1), is up-regulated over
1000-fold in planta and considerably on cellophane
membranes, and encodes a cysteine-rich secreted protein of
523 residues with eight imperfect tandem repeats of ~60
amino acids. The Cin1 sequence has no homology to known
proteins and appears to be genus-specific; however, Cin1
repeats and other repeat domains may be structurally
similar. An NMR-derived structure of the first two repeat
domains of Cin1 (Cin1-D1D2) and a low-resolution model of
the full-length protein (Cin1-FL) using SAXS data were
determined. The structure of Cin1-D1D2 reveals that each
domain comprises a core helix-loop-helix (HLH) motif as part
of a three-helix bundle, and is stabilized by two
intra-domain disulfide bonds. Cin1-D1D2 adopts a unique
protein fold as DALI and PDBeFOLD analysis identified no
structural homology. A (15)N backbone NMR dynamic analysis
of Cin1-D1D2 showed that a short stretch of the inter-domain
linker has large amplitude motions that give rise to
reciprocal domain-domain mobility. This observation was
supported by SAXS data modeling, where the scattering length
density envelope remains thick at the domain-domain
boundary, indicative of inter-domain dynamics. Cin1-FL SAXS
data models a loosely-packed arrangement of domains, rather
than the canonical parallel packing of adjacent HLH repeats
observed in α-solenoid repeat proteins. Together, these
data suggest that the repeat domains of Cin1 display a
"beads-on-a-string" organization with inherent inter-domain
flexibility that is likely to facilitate interactions with
target ligands.},
cin = {ICS-6},
ddc = {570},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {452 - Structural Biology (POF2-452)},
pid = {G:(DE-HGF)POF2-452},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000307918300006},
pubmed = {pmid:22771296},
doi = {10.1016/j.bbapap.2012.06.015},
url = {https://juser.fz-juelich.de/record/139940},
}