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==Crystal structure of the disulphide linked knotted homodimer of Psu==
<StructureSection load='4dvd' size='340' side='right'caption='[[4dvd]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4dvd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_P4 Enterobacteria phage P4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DVD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dvd OCA], [https://pdbe.org/4dvd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dvd RCSB], [https://www.ebi.ac.uk/pdbsum/4dvd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dvd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VPSU_BPP4 VPSU_BPP4] Late protein which functions to suppress polarity of amber mutations in the late genes of the P2 helper phage.
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== Publication Abstract from PubMed ==
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.

The first structure of polarity suppression protein, Psu from enterobacteria phage P4, reveals a novel fold and a knotted dimer.,Banerjee R, Nath S, Ranjan A, Khamrui S, Pani B, Sen R, Sen U J Biol Chem. 2012 Dec 28;287(53):44667-75. doi: 10.1074/jbc.M112.423202. Epub, 2012 Nov 12. PMID:23150672<ref>PMID:23150672</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Enterobacteria phage P4]]
[[Category: Large Structures]]
[[Category: Banerjee R]]
[[Category: Nath S]]
[[Category: Sen U]]