2lht

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[[Image:2lht.png|left|200px]]
 
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{{STRUCTURE_2lht| PDB=2lht | SCENE= }}
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==Solution structure of Venturia inaequalis cellophane-induced 1 protein (ViCin1) domains 1 and 2==
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<StructureSection load='2lht' size='340' side='right'caption='[[2lht]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2lht]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2LHT FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lht OCA], [https://pdbe.org/2lht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lht RCSB], [https://www.ebi.ac.uk/pdbsum/2lht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lht ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A8W3P3_VENIN A8W3P3_VENIN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Solution structure of Venturia inaequalis cellophane-induced 1 protein (ViCin1) domains 1 and 2===
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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>
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{{ABSTRACT_PUBMED_22771296}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 2lht" style="background-color:#fffaf0;"></div>
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[[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].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:022771296</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Venturia inaequalis]]
[[Category: Venturia inaequalis]]
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[[Category: Dingley, A J.]]
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[[Category: Dingley AJ]]
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[[Category: Greenwood, D R.]]
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[[Category: Greenwood DR]]
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[[Category: Mcgillivray, D J.]]
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[[Category: Mcgillivray DJ]]
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[[Category: Mesarich, C H.]]
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[[Category: Mesarich CH]]
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[[Category: Schmitz, M.]]
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[[Category: Schmitz M]]
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[[Category: Templeton, M D.]]
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[[Category: Templeton MD]]
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[[Category: Tremouilhac, P.]]
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[[Category: Tremouilhac P]]
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[[Category: Cell adhesion]]
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[[Category: Secreted repeat domain]]
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Current revision

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

PDB ID 2lht

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