2LHT

Solution structure of Venturia inaequalis cellophane-induced 1 protein (ViCin1) domains 1 and 2

Summary for 2LHT

• Entry DOI: 10.2210/pdb2lht/pdb
• NMR Information: BMRB: 17865
• Descriptor: Cellophane-induced protein 1 (1 entity in total)
• Functional Keywords: secreted repeat domain, cell adhesion
• Biological source: Venturia inaequalis (Apple scab fungus)
• Total number of polymer chains: 1
• Total formula weight: 13649.40

Authors

Mesarich, C.H.,Schmitz, M.,Tremouilhac, P.,Greenwood, D.R.,Mcgillivray, D.J.,Templeton, M.D.,Dingley, A.J. (deposition date: 2011-08-16, release date: 2012-07-18, Last modification date: 2024-10-16)

Primary citation

Mesarich, C.H.,Schmitz, M.,Tremouilhac, P.,McGillivray, D.J.,Templeton, M.D.,Dingley, A.J.
Structure, dynamics and domain organization of the repeat protein Cin1 from the apple scab fungus.
Biochim.Biophys.Acta, 1824:1118-1128, 2012

PubMed 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.

PubMed: 22771296
DOI: 10.1016/j.bbapap.2012.06.015

Experimental method

SOLUTION NMR