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http://purl.uniprot.org/citations/15288792http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15288792http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/15288792http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2004.06.038"xsd:string
http://purl.uniprot.org/citations/15288792http://purl.uniprot.org/core/author"Opella S.J."xsd:string
http://purl.uniprot.org/citations/15288792http://purl.uniprot.org/core/author"Wu C.H."xsd:string
http://purl.uniprot.org/citations/15288792http://purl.uniprot.org/core/author"Nevzorov A.A."xsd:string
http://purl.uniprot.org/citations/15288792http://purl.uniprot.org/core/author"Thiriot D.S."xsd:string
http://purl.uniprot.org/citations/15288792http://purl.uniprot.org/core/author"Zagyanskiy L."xsd:string
http://purl.uniprot.org/citations/15288792http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15288792http://purl.uniprot.org/core/name"J Mol Biol"xsd:string
http://purl.uniprot.org/citations/15288792http://purl.uniprot.org/core/pages"869-879"xsd:string
http://purl.uniprot.org/citations/15288792http://purl.uniprot.org/core/title"Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy."xsd:string
http://purl.uniprot.org/citations/15288792http://purl.uniprot.org/core/volume"341"xsd:string
http://purl.uniprot.org/citations/15288792http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15288792
http://purl.uniprot.org/citations/15288792http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15288792
http://purl.uniprot.org/uniprot/#_P03621-mappedCitation-15288792http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15288792
http://purl.uniprot.org/uniprot/P03621http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15288792