2DF5

Crystal Structure of Pf-PCP(1-204)-C

Summary for 2DF5

• Entry DOI: 10.2210/pdb2df5/pdb
• Related: 1IOF
• Descriptor: Pyrrolidone-carboxylate peptidase (2 entities in total)
• Functional Keywords: chameleon sequence, pyrococcus furiosus, pyrrolidone carboxyl peptidase, hydrolase
• Biological source: Pyrococcus furiosus
• Cellular location: Cytoplasm: O73944
• Total number of polymer chains: 4
• Total formula weight: 93549.52

Authors

Katagiri, Y.,Takano, K.,Chon, H.,Matsumura, H.,Koga, Y.,Kanaya, S. (deposition date: 2006-02-24, release date: 2007-03-06, Last modification date: 2023-10-25)

Primary citation

Takano, K.,Katagiri, Y.,Mukaiyama, A.,Chon, H.,Matsumura, H.,Koga, Y.,Kanaya, S.
Conformational contagion in a protein: structural properties of a chameleon sequence
Proteins, 68:617-625, 2007

PubMed Abstract: 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.

PubMed: 17510955
DOI: 10.1002/prot.21451

Experimental method

X-RAY DIFFRACTION (2.3 Å)