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| 001 | 139940 | ||
| 005 | 20210129212727.0 | ||
| 024 | 7 | _ | |a 10.1016/j.bbapap.2012.06.015 |2 doi |
| 024 | 7 | _ | |a 1878-1454 |2 ISSN |
| 024 | 7 | _ | |a 1570-9639 |2 ISSN |
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| 037 | _ | _ | |a FZJ-2013-05907 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Mesarich, Carl H. |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Structure, dynamics and domain organization of the repeat protein Cin1 from the apple scab fungus |
| 260 | _ | _ | |a Amsterdam [u.a.] |c 2012 |b Elsevier |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1385727047_7767 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
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| 336 | 7 | _ | |a article |2 DRIVER |
| 500 | _ | _ | |3 POF3_Assignment on 2016-02-29 |
| 520 | _ | _ | |a 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. |
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| 700 | 1 | _ | |a Schmitz, Michael |b 1 |
| 700 | 1 | _ | |a Tremouilhac, Pierre |b 2 |
| 700 | 1 | _ | |a McGillivray, Duncan J. |b 3 |
| 700 | 1 | _ | |a Templeton, Matthew D. |b 4 |
| 700 | 1 | _ | |a Dingley, Andrew |0 P:(DE-Juel1)145681 |b 5 |u fzj |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.bbapap.2012.06.015 |g Vol. 1824, no. 10, p. 1118 - 1128 |p 1118 - 1128 |n 10 |0 PERI:(DE-600)2209540-8 |t Biochimica et biophysica acta / Proteins and proteomics |v 1824 |y 2012 |x 1570-9639 |
| 856 | 4 | _ | |u http://www.sciencedirect.com/science/article/pii/S1570963912001367# |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/139940/files/FZJ-2013-05907.pdf |y Restricted |
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