2df5
Crystal Structure of Pf-PCP(1-204)-C
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| , resolution 2.30Å | |||||||
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| Activity: | Pyroglutamyl-peptidase I, with EC number 3.4.19.3 | ||||||
| Related: | 1IOF
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
Certain 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.
About this StructureAbout this Structure
2DF5 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
ReferenceReference
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
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