2dff: Difference between revisions
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==Crystal structure of Tk-RNase HII(1-204)-C== | ==Crystal structure of Tk-RNase HII(1-204)-C== | ||
<StructureSection load='2dff' size='340' side='right' caption='[[2dff]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2dff' size='340' side='right'caption='[[2dff]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2dff]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DFF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DFF FirstGlance]. <br> | <table><tr><td colspan='2'>[[2dff]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DFF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DFF FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
*[[Temp|Temp]] | *[[Temp|Temp]] | ||
== References == | == References == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Ribonuclease H]] | [[Category: Ribonuclease H]] | ||
[[Category: Chon, H]] | [[Category: Chon, H]] | ||
Revision as of 10:54, 4 March 2020
Crystal structure of Tk-RNase HII(1-204)-CCrystal structure of Tk-RNase HII(1-204)-C
Structural highlights
Function[RNH2_THEKO] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCertain sequences, known as chameleon sequences, take both alpha- and beta-conformations in natural proteins. We demonstrate that a wild chameleon sequence fused to the C-terminal alpha-helix or beta-sheet in foreign stable proteins from hyperthermophiles forms the same conformation as the host secondary structure. However, no secondary structural formation is observed when the sequence is attached to the outside of the secondary structure. These results indicate that this sequence inherently possesses an ability to make either alpha- or beta-conformation, depending on the sequentially neighboring secondary structure if little other nonlocal interaction occurs. Thus, chameleon sequences take on a satellite state through contagion by the power of a secondary structure. We propose this "conformational contagion" as a new nonlocal determinant factor in protein structure and misfolding related to protein conformational diseases. Conformational contagion in a protein: structural properties of a chameleon sequence.,Takano K, Katagiri Y, Mukaiyama A, Chon H, Matsumura H, Koga Y, Kanaya S Proteins. 2007 Aug 15;68(3):617-25. PMID:17510955[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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