1RZS

Solution structure of P22 Cro

1RZS の概要

• エントリーDOI: 10.2210/pdb1rzs/pdb
• NMR情報: BMRB: 6185
• 分子名称: Regulatory protein cro (1 entity in total)
• 機能のキーワード: helix-turn-helix, dna-binding protein, structural evolution, transcription
• 由来する生物種: Enterobacteria phage P22
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6837.77

構造登録者

Newlove, T.,Konieczka, J.H.,Cordes, M.H. (登録日: 2003-12-28, 公開日: 2004-06-01, 最終更新日: 2024-05-22)

主引用文献

Newlove, T.,Konieczka, J.H.,Cordes, M.H.
Secondary structure switching in Cro protein evolution.
STRUCTURE, 12:569-581, 2004

PubMed Abstract: We report the solution structure of the Cro protein from bacteriophage P22. Comparisons of its sequence and structure to those of lambda Cro strongly suggest an alpha-to-beta secondary structure switching event during Cro evolution. The folds of P22 Cro and lambda Cro share a three alpha helix fragment comprising the N-terminal half of the domain. However, P22 Cro's C terminus folds as two helices, while lambda Cro's folds as a beta hairpin. The all-alpha fold found for P22 Cro appears to be ancestral, since it also occurs in cI proteins, which are anciently duplicated paralogues of Cro. PSI-BLAST and transitive homology analyses strongly suggest that the sequences of P22 Cro and lambda Cro are globally homologous despite encoding different folds. The alpha+beta fold of lambda Cro therefore likely evolved from its all-alpha ancestor by homologous secondary structure switching, rather than by nonhomologous replacement of both sequence and structure.

PubMed: 15062080
DOI: 10.1016/j.str.2004.02.024

実験手法

SOLUTION NMR