Filamentous Phage Studied by Magic-Angle Spinning NMR: Resonance Assignment and Secondary Structure of the Coat Protein in Pf1
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- 作者：Amir Goldbourt ; Benjamin J. Gross ; Loren A. Day ; Ann E. McDermott
- 刊名：Journal of the American Chemical Society
- 出版年：2007
- 出版时间：February 28, 2007
- 年：2007
- 卷：129
- 期：8
- 页码：2338 - 2344
- 全文大小：251K
- 年卷期：v.129,no.8(February 28, 2007)
- ISSN：1520-5126
文摘
Assignments are presented for resonances in the magic-angle spinning solid-state NMR spectraof the major coat protein subunit of the filamentous bacteriophage Pf1. NMR spectra were collected onuniformly 13C and 15N isotopically enriched, polyethylene glycol precipitated samples of fully infectious andhydrated phage. Site-specific assignments were achieved for 231 of the 251 labeled atoms (92%) of the46-residue-long coat protein, including 136 of the 138 backbone atoms, by means of two- andthree-dimensional 15N and 13C correlation experiments. A single chemical shift was observed for the vastmajority of atoms, suggesting a single conformation for the 7300 subunits in the 36 MDa virion in its high-temperature form. On the other hand, multiple chemical shifts were observed for the C
, C
, and C
atomsof T5 in the helix terminus and the C and C atoms of M42 in the DNA interaction domain. The chemicalshifts of the backbone atoms indicate that the coat protein conformation involves a 40-residue continuous-helix extending from residue 6 to the C-terminus.
, C, and C atomsof T5 in the helix terminus and the C and C atoms of M42 in the DNA interaction domain. The chemicalshifts of the backbone atoms indicate that the coat protein conformation involves a 40-residue continuous-helix extending from residue 6 to the C-terminus.