1pjf

<StructureSection load='1pjf' size='340' side='right' caption='[[1pjf]], [[NMR_Ensembles_of_Models | 27 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1pjf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_pf1 Pseudomonas phage pf1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PJF FirstGlance]. <br>

</td></tr><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=1pjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pjf OCA], [http://pdbe.org/1pjf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pjf RCSB], [http://www.ebi.ac.uk/pdbsum/1pjf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pjf ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CAPSD_BPPF1 CAPSD_BPPF1]] Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (By similarity).

The atomic resolution structure of Pf1 coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles in solution is compared to the structures previously determined by X-ray fiber and neutron diffraction, the structure of its membrane-bound form, and the structure of fd coat protein. These structural comparisons provide insights into several biological properties, differences between class I and class II filamentous bacteriophages, and the assembly process. The six N-terminal amino acid residues adopt an unusual "double hook" conformation on the outside of the bacteriophage particle. The solid-state NMR results indicate that at 30 degrees C, some of the coat protein subunits assume a single, fully structured conformation, and some have a few mobile residues that provide a break between two helical segments, in agreement with structural models from X-ray fiber and neutron diffraction, respectively. The atomic resolution structure determined by solid-state NMR for residues 7-14 and 18-46, which excludes the N-terminal double hook and the break between the helical segments, but encompasses more than 80% of the backbone including the distinct kink at residue 29, agrees with that determined by X-ray fiber diffraction with an RMSD value of 2.0 A. The symmetry and distance constraints determined by X-ray fiber and neutron diffraction enable the construction of an accurate model of the bacteriophage particle from the coordinates of the coat protein monomers.

 

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== References ==

[[Category: Pseudomonas phage pf1]]

[[Category: Nevzorov, A A]]

[[Category: Opella, S J]]

[[Category: Thiriot, D S]]

[[Category: Wu, C H]]

[[Category: Zagyanskiy, L]]

[[Category: Viral protein]]