5X15

Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase ES inhibitor RraA protein family

Summary for 5X15

• Entry DOI: 10.2210/pdb5x15/pdb
• Descriptor: Putative transferase (1 entity in total)
• Functional Keywords: rnase es inhibitor, streptomyces coelicolor, rraas2, rraa protein family, transferase, transferase inhibitor
• Biological source: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
• Total number of polymer chains: 3
• Total formula weight: 88653.40

Authors

Park, N.,Jo, I.,Ha, N.-C. (deposition date: 2017-01-24, release date: 2017-05-17, Last modification date: 2024-03-20)

Primary citation

Park, N.,Heo, J.,Song, S.,Jo, I.,Lee, K.,Ha, N.C.
Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase E inhibitor RraA protein family
J. Microbiol., 55:388-395, 2017

PubMed Abstract: Bacterial ribonuclease E (RNase E) plays a crucial role in the processing and decay of RNAs. A small protein named RraA negatively regulates the activity of RNase E via protein-protein interaction in various bacteria. Recently, RraAS1 and RraAS2, which are functional homologs of RraA from Escherichia coli, were identified in the Gram-positive species Streptomyces coelicolor. RraAS1 and RraAS2 inhibit RNase ES ribonuclease activity in S. coelicolor. RraAS1 and RraAS2 have a C-terminal extension region unlike typical bacterial RraA proteins. In this study, we present the crystal structure of RraAS2, exhibiting a hexamer arranged in a dimer of trimers, consistent with size exclusion chromatographic results. Importantly, the C-terminal extension region formed a long α-helix at the junction of the neighboring subunit, which is similar to the trimeric RraA orthologs from Saccharomyces cerevisiae. Truncation of the C-terminal extension region resulted in loss of RNase ES inhibition, demonstrating its crucial role. Our findings present the first bacterial RraA that has a hexameric assembly with a C-terminal extension α-helical region, which plays an essential role in the regulation of RNase ES activity in S. coelicolor.

PubMed: 28455590
DOI: 10.1007/s12275-017-7053-8

Experimental method

X-RAY DIFFRACTION (3.094 Å)