2lht
From Proteopedia
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- | [[ | + | ==Solution structure of Venturia inaequalis cellophane-induced 1 protein (ViCin1) domains 1 and 2== |
+ | <StructureSection load='2lht' size='340' side='right' caption='[[2lht]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2lht]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Venturia_inaequalis Venturia inaequalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LHT FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CIN1, ViCin1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5025 Venturia inaequalis])</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lht RCSB], [http://www.ebi.ac.uk/pdbsum/2lht PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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 alpha-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. | ||
- | + | Structure, dynamics and domain organization of the repeat protein Cin1 from the apple scab fungus.,Mesarich CH, Schmitz M, Tremouilhac P, McGillivray DJ, Templeton MD, Dingley AJ Biochim Biophys Acta. 2012 Oct;1824(10):1118-28. Epub 2012 Jul 4. PMID:22771296<ref>PMID:22771296</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Venturia inaequalis]] | [[Category: Venturia inaequalis]] | ||
[[Category: Dingley, A J.]] | [[Category: Dingley, A J.]] |
Revision as of 06:58, 9 June 2014
Solution structure of Venturia inaequalis cellophane-induced 1 protein (ViCin1) domains 1 and 2
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