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Insights from multiple structures of the shell proteins from the β-carboxysome

  1. Shiho Tanaka1,
  2. Michael R. Sawaya2,
  3. Martin Phillips1,
  4. Todd O. Yeates1,2,3,*

Article first published online: 2 DEC 2008

DOI: 10.1002/pro.14

Issue

Protein Science

Protein Science

Volume 18, Issue 1, pages 108–120, January 2009

Additional Information

How to Cite

Tanaka, S., Sawaya, M. R., Phillips, M. and Yeates, T. O. (2009), Insights from multiple structures of the shell proteins from the β-carboxysome. Protein Science, 18: 108–120. doi: 10.1002/pro.14

Author Information

  1. 1

    Department of Chemistry and Biochemistry, University of California, Los Angeles, California

  2. 2

    UCLA-DOE Institute for Genomics and Proteomics, Los Angeles, California

  3. 3

    UCLA Molecular Biology Institute, Los Angeles, California

*UCLA Department of Chemistry and Biochemistry, 611 Charles Young Dr., Los Angeles, CA 90095-1569

Publication History

  1. Issue published online: 16 DEC 2008
  2. Article first published online: 2 DEC 2008
  3. Accepted manuscript online: 2 DEC 2008 12:00AM EST
  4. Manuscript Accepted: 15 OCT 2008
  5. Manuscript Revised: 14 OCT 2008
  6. Manuscript Received: 29 JUL 2008

Funded by

  • BER Program of the Department of Energy Office of Science

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FilenameFormatSizeDescription
PRO_14_sm_SuppFigures1-3.doc8534KSupporting Information Figure 1. (A) The residues around the pore of the hexamer at the 6-fold axis of symmetry. Six Ser 39 residues at the narrowest point at the 6-fold from the CcmK1 hexamer and the Form 1 CcmK2d hexamer are compared side by side. Six Lys 36 residues of the opposite face of the CcmK1 hexamer are indicated. The color gradient of the surface diagram indicates negative electrostatic potential in red and positive electrostatic potential in blue. (B) The arrangement of two Lys 36 residues from adjacent subunits and Glu 35 is shown. (C) The location of Ser 39 and Lys 36 are indicated in the side view of the CcmK1 hexamer. Supporting Information Figure 2. Reconstructed electrospray LC/MS spectrum of the CcmK1 protein. The calculated molecular weight from the sequence of the full length CcmK1 protein without Met 1 including the expression tag is 13249.1 daltons. The dominant peak at 13252.0 daltons confirms that the protein is full length. Supporting Information Figure 3. Hydrophobic character of the two sides of the CcmK1 molecular layer. The color gradient indicates greater hydrophobicity in red and lower hydrophobicity in blue.

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