2BH8

Combinatorial Protein 1b11

2BH8 の概要

• エントリーDOI: 10.2210/pdb2bh8/pdb
• 関連するPDBエントリー: 1MJC 3MEF
• 分子名称: 1B11 (2 entities in total)
• 機能のキーワード: transcription, molecular evolution, unique architecture, ob-fold, activator, dna-binding, transcription regulation, rna- binding, ribosomal protein, phosphorylation
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21477.87

構造登録者

De Bono, S.,Riechmann, L.,Girard, E.,Williams, R.L.,Winter, G. (登録日: 2005-01-07, 公開日: 2005-02-07, 最終更新日: 2024-05-08)

主引用文献

De Bono, S.,Riechmann, L.,Girard, E.,Williams, R.L.,Winter, G.
A Segment of Cold Shock Protein Directs the Folding of a Combinatorial Protein
Proc.Natl.Acad.Sci.USA, 102:1396-, 2005

PubMed Abstract: It has been suggested that protein domains evolved by the non-homologous recombination of building blocks of subdomain size. In earlier work we attempted to recapitulate domain evolution in vitro. We took a polypeptide segment comprising three beta-strands in the monomeric, five-stranded beta-barrel cold shock protein (CspA) of Escherichia coli as a building block. This segment corresponds to a complete exon in homologous eukaryotic proteins and includes residues that nucleate folding in CspA. We recombined this segment at random with fragments of natural proteins and succeeded in generating a range of folded chimaeric proteins. We now present the crystal structure of one such combinatorial protein, 1b11, a 103-residue polypeptide that includes segments from CspA and the S1 domain of the 30S ribosomal subunit of E. coli. The structure reveals a segment-swapped, six-stranded beta-barrel of unique architecture that assembles to a tetramer. Surprisingly, the CspA segment retains its structural identity in 1b11, recapitulating its original fold and deforming the structure of the S1 segment as necessary to complete a barrel. Our work provides structural evidence that (i) random shuffling of nonhomologous polypeptide segments can lead to folded proteins and unique architectures, (ii) many structural features of the segments are retained, and (iii) some segments can act as templates around which the rest of the protein folds.

PubMed: 15671167
DOI: 10.1073/PNAS.0407298102

実験手法

X-RAY DIFFRACTION (1.9 Å)