3MW6

Crystal structure of NMB1681 from Neisseria meningitidis MC58, a FinO-like RNA chaperone

Replaces:  2HXJ

Summary for 3MW6

• Entry DOI: 10.2210/pdb3mw6/pdb
• Related: 2HXJ
• Descriptor: uncharacterized protein NMB1681, GLYCEROL (3 entities in total)
• Functional Keywords: structural genomics, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• Biological source: Neisseria meningitidis
• Total number of polymer chains: 6
• Total formula weight: 95693.55

Authors

Tan, K.,Zhou, M.,Duggan, E.,Abdullah, J.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2010-05-05, release date: 2010-06-23, Last modification date: 2024-11-27)

Primary citation

Chaulk, S.,Lu, J.,Tan, K.,Arthur, D.C.,Edwards, R.A.,Frost, L.S.,Joachimiak, A.,Glover, J.N.
N. meningitidis 1681 is a member of the FinO family of RNA chaperones.
Rna Biol., 7:112-119, 2010

PubMed Abstract: The conjugative transfer of F-like plasmids between bacteria is regulated by the plasmid-encoded RNA chaperone, FinO, which facilitates sense - antisense RNA interactions to regulate plasmid gene expression. FinO was thought to adopt a unique structure, however many putative homologs have been identified in microbial genomes and are considered members of the FinO_conjugation_repressor superfamily. We were interested in determining whether other members were also able to bind RNA and promote duplex formation, suggesting that this motif does indeed identify a putative RNA chaperone. We determined the crystal structure of the N. meningitidis MC58 protein NMB1681. It revealed striking similarity to FinO, with a conserved fold and a large, positively charged surface that could function in RNA interactions. Using assays developed to study FinO-FinP sRNA interactions, NMB1681, like FinO, bound tightly to FinP RNA stem-loops with short 5' and 3' single-stranded tails but not to ssRNA. It also was able to catalyze strand exchange between an RNA duplex and a complementary single-strand, and facilitated duplexing between complementary RNA hairpins. Finally, NMB1681 was able to rescue a finO deficiency and repress F plasmid conjugation. This study strongly suggests that NMB1681 is a FinO-like RNA chaperone that likely regulates gene expression through RNA-based mechanisms in N. meningitidis.

PubMed: 21045552

Experimental method

X-RAY DIFFRACTION (2.209 Å)