1REG

CRYSTAL STRUCTURE OF THE T4 REGA TRANSLATIONAL REGULATOR PROTEIN AT 1.9 ANGSTROMS RESOLUTION

Summary for 1REG

• Entry DOI: 10.2210/pdb1reg/pdb
• Descriptor: T4 REGA (2 entities in total)
• Functional Keywords: translational regulator protein
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 2
• Total formula weight: 29286.30

Authors

Kang, C.,Rich, A. (deposition date: 1995-01-11, release date: 1996-01-01, Last modification date: 2024-02-14)

Primary citation

Kang, C.,Chan, R.,Berger, I.,Lockshin, C.,Green, L.,Gold, L.,Rich, A.
Crystal structure of the T4 regA translational regulator protein at 1.9 A resolution.
Science, 268:1170-1173, 1995

PubMed Abstract: The translational regulator protein regA is encoded by the T4 bacteriophage and binds to a region of messenger RNA (mRNA) that includes the initiator codon. RegA is unusual in that it represses the translation of about 35 early T4 mRNAs but does not affect nearly 200 other mRNAs. The crystal structure of regA was determined at 1.9 A resolution; the protein was shown to have an alpha-helical core and two regions with antiparallel beta sheets. One of these beta sheets has four antiparallel strands and has some sequence homology to RNP-1 and RNP-2, which are believed to be RNA-binding motifs and are found in a number of known RNA-binding proteins. Structurally guided mutants may help to uncover the basis for this variety of RNA interaction.

PubMed: 7761833

Experimental method

X-RAY DIFFRACTION (1.9 Å)