2lht: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 2lht is ~~ON HOLD until Paper~~ Publication

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

== Structural highlights ==

<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>

</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>

<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>

</table>

== Function ==

[https://www.uniprot.org/uniprot/A8W3P3_VENIN A8W3P3_VENIN]

== 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.

~~Authors: Mesarich~~, ~~C.H~~., Schmitz, M., Tremouilhac, P~~., Greenwood~~, ~~D.R., Mcgillivray, D.J.~~, Templeton, M.~~D., Dingley, A~~.J.

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>

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Venturia inaequalis]]

[[Category: Dingley AJ]]

[[Category: Greenwood DR]]

[[Category: Mcgillivray DJ]]

[[Category: Mesarich CH]]

[[Category: Schmitz M]]

[[Category: Templeton MD]]

[[Category: Tremouilhac P]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2lht is ON HOLD  until Paper Publication
+==Solution structure of Venturia inaequalis cellophane-induced 1 protein (ViCin1) domains 1 and 2==
+<StructureSection load='2lht' size='340' side='right'caption='[[2lht]]' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A8W3P3_VENIN A8W3P3_VENIN]
+<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.
-Authors: Mesarich, C.H., Schmitz, M., Tremouilhac, P., Greenwood, D.R., Mcgillivray, D.J., Templeton, M.D., Dingley, A.J.
+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>
-Description: Solution structure of Venturia inaequalis cellophane-induced 1 protein (ViCin1) domains 1 and 2
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2lht" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Venturia inaequalis]]
+[[Category: Dingley AJ]]
+[[Category: Greenwood DR]]
+[[Category: Mcgillivray DJ]]
+[[Category: Mesarich CH]]
+[[Category: Schmitz M]]
+[[Category: Templeton MD]]
+[[Category: Tremouilhac P]]