1ql2 Citations

The molecular structure and structural transition of the alpha-helical capsid in filamentous bacteriophage Pf1.

Acta Crystallogr. D Biol. Crystallogr. 56 137-50 (2000)
Related entries: 1ifd, 1ql1, 2ifm, 2ifn, 2ifo, 3ifm, 4ifm

Cited: 15 times
EuropePMC logo PMID: 10666593

Abstract

The major coat protein in the capsid of Pf1 filamentous bacteriophage (Inovirus) forms a helical assembly of about 7000 identical protein subunits, each of which contains 46 amino-acid residues and can be closely approximated by a single gently curved alpha-helix. Since the viral DNA occupies the core of the tubular capsid and appears to make no significant specific interactions with the capsid proteins, the capsid is a simple model system for the study of the static and dynamic properties of alpha-helix assembly. The capsid undergoes a reversible temperature-induced structural transition at about 283 K between two slightly different helix forms. The two forms can coexist without an intermediate state, consistent with a first-order structural phase transition. The molecular model of the higher temperature form was refined using improved X-ray fibre diffraction data and new refinement and validation methods. The refinement indicates that the two forms are related by a change in the orientation of the capsid subunits within the virion, without a significant change in local conformation of the subunits. On the higher temperature diffraction pattern there is a region of observed intensity that is not consistent with a simple helix of identical subunits; it is proposed that the structure involves groups of three subunits which each have a slightly different orientation within the group. The grouping of subunits suggests that a change in subunit libration frequency could be the basis of the Pf1 structural transition; calculations from the model are used to explore this idea.

Articles - 1ql2 mentioned but not cited (1)

  1. Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR. Straus SK, Scott WR, Schwieters CD, Marvin DA. Eur. Biophys. J. 40 221-234 (2011)


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Articles citing this publication (13)

  1. Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy. Thiriot DS, Nevzorov AA, Zagyanskiy L, Wu CH, Opella SJ. J. Mol. Biol. 341 869-879 (2004)
  2. Conformational dynamics of an intact virus: order parameters for the coat protein of Pf1 bacteriophage. Lorieau JL, Day LA, McDermott AE. Proc. Natl. Acad. Sci. U.S.A. 105 10366-10371 (2008)
  3. Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membrane. Marvin DA, Welsh LC, Symmons MF, Scott WR, Straus SK. J. Mol. Biol. 355 294-309 (2006)
  4. Structural basis of the temperature transition of Pf1 bacteriophage. Thiriot DS, Nevzorov AA, Opella SJ. Protein Sci. 14 1064-1070 (2005)
  5. The protein capsid of filamentous bacteriophage PH75 from Thermus thermophilus. Pederson DM, Welsh LC, Marvin DA, Sampson M, Perham RN, Yu M, Slater MR. J. Mol. Biol. 309 401-421 (2001)
  6. Identification and specificity of pilus adsorption proteins of filamentous bacteriophages infecting Pseudomonas aeruginosa. Holland SJ, Sanz C, Perham RN. Virology 345 540-548 (2006)
  7. Intersubunit hydrophobic interactions in Pf1 filamentous phage. Goldbourt A, Day LA, McDermott AE. J. Biol. Chem. 285 37051-37059 (2010)
  8. A structural model for the single-stranded DNA genome of filamentous bacteriophage Pf1. Tsuboi M, Tsunoda M, Overman SA, Benevides JM, Thomas GJ. Biochemistry 49 1737-1743 (2010)
  9. Orientation and interactions of an essential tryptophan (Trp-38) in the capsid subunit of Pf3 filamentous virus. Tsuboi M, Overman SA, Nakamura K, Rodriguez-Casado A, Thomas GJ. Biophys. J. 84 1969-1976 (2003)
  10. Raman spectroscopy of proteins and nucleoproteins. Nemecek D, Stepanek J, Thomas GJ. Curr Protoc Protein Sci Chapter 17 Unit17.8 (2013)
  11. Secondary structural analysis of proteins based on (13)C chemical shift assignments in unresolved solid-state NMR spectra enhanced by fragmented structure database. Ikeda K, Egawa A, Fujiwara T. J. Biomol. NMR 55 189-200 (2013)
  12. Automated determination of fibrillar structures by simultaneous model building and fiber diffraction refinement. Potrzebowski W, André I. Nat. Methods 12 679-684 (2015)
  13. Cryo-electron microscopy structure of the filamentous bacteriophage IKe. Xu J, Dayan N, Goldbourt A, Xiang Y. Proc. Natl. Acad. Sci. U.S.A. 116 5493-5498 (2019)


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