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The MotA protein from bacteriophage T4 contains two domains. Preliminary structural analysis by X-ray diffraction and nuclear magnetic resonance.

Publication ,  Journal Article
Finnin, MS; Hoffman, DW; Kreuzer, KN; Porter, SJ; Schmidt, RP; White, SW
Published in: J Mol Biol
July 5, 1993

Controlled protease cleavage experiments and N-terminal sequence analyses were used to show that the transcriptional activator MotA from bacteriophage T4 has a two-domain structure. The N and C-terminal domains have M(r) values of 10,300 and 11,800, respectively, and were separately cloned and overexpressed in Escherichia coli. One and two-dimensional NMR spectroscopy indicate that both domains have stably folded structures and contain extensive secondary structure. The N-terminal domain is substantially alpha-helical, whereas the C-terminal domain has a high content of beta-strand. The N-terminal domain has been crystallized under three different conditions, all with the space group P3(1(2))21 and similar unit cell dimensions. The best crystals are grown from ammonium sulfate, have cell dimensions a = b = 46.7 A, c = 139.6 A, and diffract to beyond 2.4 A. The high quality of the NMR and diffraction data will allow a complete structural analysis of MotA by a combination of these techniques.

Duke Scholars

Published In

J Mol Biol

DOI

ISSN

0022-2836

Publication Date

July 5, 1993

Volume

232

Issue

1

Start / End Page

301 / 304

Location

Netherlands

Related Subject Headings

  • X-Ray Diffraction
  • Viral Proteins
  • Transcription Factors
  • Regulatory Sequences, Nucleic Acid
  • Peptide Fragments
  • Molecular Sequence Data
  • Magnetic Resonance Spectroscopy
  • DNA-Binding Proteins
  • DNA Replication
  • Crystallography
 

Citation

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Finnin, M. S., Hoffman, D. W., Kreuzer, K. N., Porter, S. J., Schmidt, R. P., & White, S. W. (1993). The MotA protein from bacteriophage T4 contains two domains. Preliminary structural analysis by X-ray diffraction and nuclear magnetic resonance. J Mol Biol, 232(1), 301–304. https://doi.org/10.1006/jmbi.1993.1384
Finnin, M. S., D. W. Hoffman, K. N. Kreuzer, S. J. Porter, R. P. Schmidt, and S. W. White. “The MotA protein from bacteriophage T4 contains two domains. Preliminary structural analysis by X-ray diffraction and nuclear magnetic resonance.J Mol Biol 232, no. 1 (July 5, 1993): 301–4. https://doi.org/10.1006/jmbi.1993.1384.
Finnin MS, Hoffman DW, Kreuzer KN, Porter SJ, Schmidt RP, White SW. The MotA protein from bacteriophage T4 contains two domains. Preliminary structural analysis by X-ray diffraction and nuclear magnetic resonance. J Mol Biol. 1993 Jul 5;232(1):301–4.
Finnin, M. S., et al. “The MotA protein from bacteriophage T4 contains two domains. Preliminary structural analysis by X-ray diffraction and nuclear magnetic resonance.J Mol Biol, vol. 232, no. 1, July 1993, pp. 301–04. Pubmed, doi:10.1006/jmbi.1993.1384.
Finnin MS, Hoffman DW, Kreuzer KN, Porter SJ, Schmidt RP, White SW. The MotA protein from bacteriophage T4 contains two domains. Preliminary structural analysis by X-ray diffraction and nuclear magnetic resonance. J Mol Biol. 1993 Jul 5;232(1):301–304.
Journal cover image

Published In

J Mol Biol

DOI

ISSN

0022-2836

Publication Date

July 5, 1993

Volume

232

Issue

1

Start / End Page

301 / 304

Location

Netherlands

Related Subject Headings

  • X-Ray Diffraction
  • Viral Proteins
  • Transcription Factors
  • Regulatory Sequences, Nucleic Acid
  • Peptide Fragments
  • Molecular Sequence Data
  • Magnetic Resonance Spectroscopy
  • DNA-Binding Proteins
  • DNA Replication
  • Crystallography