3RX6
Crystal structure of Polarity Suppression protein from Enterobacteria phage P4
Summary for 3RX6
| Entry DOI | 10.2210/pdb3rx6/pdb |
| Descriptor | Polarity suppression protein, MERCURY (II) ION, IODIDE ION, ... (5 entities in total) |
| Functional Keywords | all alpha protein, transcription termination inhibitor, rho binding, capsid decoration protein of bacteriophage p4, transcription termination inhibition, transcription terminator rho helicase, enterobacteria phage p4 capsid, transcription regulator |
| Biological source | Enterobacteria phage P4 |
| Total number of polymer chains | 1 |
| Total formula weight | 21842.70 |
| Authors | Banerjee, R.,Nath, S.,Khamrui, S.,Sen, R.,Sen, U. (deposition date: 2011-05-10, release date: 2012-07-25, Last modification date: 2024-03-20) |
| Primary citation | Banerjee, R.,Nath, S.,Ranjan, A.,Khamrui, S.,Pani, B.,Sen, R.,Sen, U. The first structure of polarity suppression protein, Psu from enterobacteria phage P4, reveals a novel fold and a knotted dimer J.Biol.Chem., 287:44667-44675, 2012 Cited by PubMed Abstract: Psu is a capsid decoration protein of bacteriophage P4 and acts as an antiterminator of Rho-dependent transcription termination in bacteria. So far, no structures have been reported for the Psu protein or its homologues. Here, we report the first structure of Psu solved by the Hg(2+) single wavelength anomalous dispersion method, which reveals that Psu exists as a knotted homodimer and is first of its kind in nature. Each monomer of Psu attains a novel fold around a tight coiled-coil motif. CD spectroscopy and the structure of an engineered disulfide-bridged Psu derivative reveal that the protein folds reversibly and reassembles by itself into the knotted dimeric conformation without the requirement of any chaperone. This structure would help to explain the functional properties of the protein and can be used as a template to design a minimal peptide fragment that can be used as a drug against Rho-dependent transcription termination in bacteria. PubMed: 23150672DOI: 10.1074/jbc.M112.423202 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.039 Å) |
Structure validation
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