1RZS

Solution structure of P22 Cro

Summary for 1RZS

• Entry DOI: 10.2210/pdb1rzs/pdb
• NMR Information: BMRB: 6185
• Descriptor: Regulatory protein cro (1 entity in total)
• Functional Keywords: helix-turn-helix, dna-binding protein, structural evolution, transcription
• Biological source: Enterobacteria phage P22
• Total number of polymer chains: 1
• Total formula weight: 6837.77

Authors

Newlove, T.,Konieczka, J.H.,Cordes, M.H. (deposition date: 2003-12-28, release date: 2004-06-01, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

SOLUTION NMR