3VU3

Crystal structure of the Hfq and catalase HPII complex

Summary for 3VU3

• Entry DOI: 10.2210/pdb3vu3/pdb
• Descriptor: Catalase HPII, Protein hfq, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: hydroperoxidase hpii, rna binding protein, oxidoreductase-rna binding protein complex, oxidoreductase/rna binding protein
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm (Probable): P21179
• Total number of polymer chains: 7
• Total formula weight: 151964.06

Authors

Watanabe, M.,Yonekura, K. (deposition date: 2012-06-15, release date: 2013-11-20, Last modification date: 2024-10-09)

Primary citation

Yonekura, K.,Watanabe, M.,Kageyama, Y.,Hirata, K.,Yamamoto, M.,Maki-Yonekura, S.
Post-Transcriptional Regulator Hfq Binds Catalase HPII: Crystal Structure of the Complex
Plos One, 8:e78216-e78216, 2013

PubMed Abstract: We report a crystal structure of Hfq and catalase HPII from Escherichia coli. The post-transcriptional regulator Hfq plays a key role in the survival of bacteria under stress. A small non-coding RNA (sRNA) DsrA is required for translation of the stationary phase sigma factor RpoS, which is the central regulator of the general stress response. Hfq facilitates efficient translation of rpoS mRNA, which encodes RpoS. Hfq helps in the function of other specific proteins involved in RNA processing, indicating its versatility in the cell. However, structural information regarding its interactions with partners is missing. Here we obtained crystals of Hfq and HPII complexes from cell lysates following attempts to overexpress a foreign membrane protein. HPII is one of two catalases in E. coli and its mRNA is transcribed by an RNA polymerase holoenzyme containing RpoS, which in turn is under positive control of small non-coding RNAs and of the RNA chaperone Hfq. This sigma factor is known to have a pronounced effect on the expression of HPII. The crystal structure reveals that a Hfq hexamer binds each subunit of a HPII tetramer. Each subunit of the Hfq hexamer exhibits a unique binding mode with HPII. The hexamer of Hfq interacts via its distal surface. The proximal and distal surfaces are known to specifically bind different sRNAs, and binding of HPII could affect Hfq function. Hfq-HPII complexation has no effect on catalase HPII activity.

PubMed: 24223139
DOI: 10.1371/journal.pone.0078216

Experimental method

X-RAY DIFFRACTION (2.85 Å)