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| | ==Crystal structure of the disulphide linked knotted homodimer of Psu== | | ==Crystal structure of the disulphide linked knotted homodimer of Psu== |
| - | <StructureSection load='4dvd' size='340' side='right' caption='[[4dvd]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='4dvd' size='340' side='right'caption='[[4dvd]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dvd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpp4 Bpp4]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DVD FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rx6|3rx6]]</td></tr> | + | </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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">psu ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10680 BPP4])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dvd OCA], [http://pdbe.org/4dvd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dvd RCSB], [http://www.ebi.ac.uk/pdbsum/4dvd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dvd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [[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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpp4]] | + | [[Category: Enterobacteria phage P4]] |
| - | [[Category: Banerjee, R]] | + | [[Category: Large Structures]] |
| - | [[Category: Nath, S]] | + | [[Category: Banerjee R]] |
| - | [[Category: Sen, U]] | + | [[Category: Nath S]] |
| - | [[Category: All alpha protein]] | + | [[Category: Sen U]] |
| - | [[Category: Capsid decoration protein of bacteriophage p4]]
| + | |
| - | [[Category: Rho binding]]
| + | |
| - | [[Category: Transcription regulator]]
| + | |
| - | [[Category: Transcription termination inhibitor]]
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| - | [[Category: Transcription terminator rho helicase]]
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| Structural highlights
Function
[VPSU_BPP4] Late protein which functions to suppress polarity of amber mutations in the late genes of the P2 helper phage.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2012 Dec 28;287(53):44667-75. doi: 10.1074/jbc.M112.423202. Epub, 2012 Nov 12. PMID:23150672 doi:10.1074/jbc.M112.423202
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