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.
Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy
Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy
Ivan V. Sergeyev, Loren A. Day, Amir Goldbourt and Ann E. McDermott
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2043062/aop/images/medium/ja-2011-043062_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2043062
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/EeKgo5vg1K0
nmrlearner
Journal club
0
11-30-2011 10:45 PM
Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy.
Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy.
Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy.
J Am Chem Soc. 2011 Aug 22;
Authors: Sergeyev IV, Day LA, Goldbourt A, McDermott AE
Abstract
Solid state NMR spectra, including dynamic nuclear polarization enhanced 400 MHz spectra acquired at 100K, as well as non-DNP spectra at a variety of field strengths and...
nmrlearner
Journal club
0
08-23-2011 04:03 PM
Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Eur Biophys J. 2011 Mar;40(3):221-34
Authors: Straus SK, Scott WR, Schwieters CD, Marvin DA
Filamentous bacteriophages (filamentous bacterial viruses or Inovirus) are simple and well-characterised macromolecular assemblies that are widely used in molecular biology and biophysics, both as paradigms for studying basic biological questions and as...
nmrlearner
Journal club
0
06-15-2011 01:15 PM
[NMR paper] Structure of the coat protein in fd filamentous bacteriophage particles determined by
Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.
Related Articles Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.
Proc Natl Acad Sci U S A. 2003 May 27;100(11):6458-63
Authors: Zeri AC, Mesleh MF, Nevzorov AA, Opella SJ
The atomic resolution structure of fd coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles differs from that previously determined...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[NMR paper] Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscop
Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy.
Related Articles Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy.
Nature. 2002 Nov 7;420(6911):98-102
Authors: Castellani F, van Rossum B, Diehl A, Schubert M, Rehbein K, Oschkinat H
The determination of a representative set of protein structures is a chief aim in structural genomics. Solid-state NMR may have a crucial role in structural investigations of those proteins that do not easily form crystals or are not...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by sol
Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR.
Biochemistry. 1996 Apr 23;35(16):5145-57
Authors: Williams KA, Farrow NA, Deber CM, Kay LE
The structure and dynamics of the 53-residue filamentous bacteriophage IKe major coat protein in fully protonated myristoyllysophosphatidylglycerol (MPG)...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] NMR studies of the major coat protein of bacteriophage M13. Structural information of
NMR studies of the major coat protein of bacteriophage M13. Structural information of gVIIIp in dodecylphosphocholine micelles.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR studies of the major coat protein of bacteriophage M13. Structural information of gVIIIp in dodecylphosphocholine micelles.
Eur J Biochem. 1995 Sep 1;232(2):490-500
Authors: Papavoine CH, Aelen JM, Konings RN, Hilbers CW, Van de Ven FJ
The membrane-bound...
nmrlearner
Journal club
0
08-22-2010 03:50 AM
[NMR paper] NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat pr
NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
Related Articles NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
Science. 1991 May 31;252(5010):1303-5
Authors: Shon KJ, Kim Y, Colnago LA, Opella SJ
Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from the membrane environment of the cell, where it spans the phospholipid bilayer, to the newly extruded virus particles....