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The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity

  1. Ulrich Weininger1,†,
  2. Roman P. Jakob2,†,
  3. Michael Kovermann1,
  4. Jochen Balbach1,
  5. Franz X. Schmid2,*

Article first published online: 28 OCT 2009

DOI: 10.1002/pro.277

Issue

Protein Science

Protein Science

Volume 19, Issue 1, pages 6–18, January 2010

Additional Information

How to Cite

Weininger, U., Jakob, R. P., Kovermann, M., Balbach, J. and Schmid, F. X. (2010), The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity. Protein Science, 19: 6–18. doi: 10.1002/pro.277

Author Information

  1. 1

    Institut für Physik, Biophysik, and Mitteldeutsches Zentrum für Struktur und Dynamik der Proteine (MZP), Martin-Luther-Universität Halle-Wittenberg, D-06120 Halle(Saale), Germany

  2. 2

    Laboratorium für Biochemie, Universität Bayreuth, D-95440 Bayreuth, Germany

  1. †

    Ulrich Weininger and Roman P. Jakob contributed equally to this work.

*Biochemie, Universität Bayreuth, D-95440 Bayreuth, Germany

Publication History

  1. Issue published online: 6 JAN 2010
  2. Article first published online: 28 OCT 2009
  3. Accepted manuscript online: 28 OCT 2009 12:00AM EST
  4. Manuscript Accepted: 6 OCT 2009
  5. Manuscript Revised: 5 OCT 2009
  6. Manuscript Received: 20 AUG 2009

Funded by

  • Fonds der Chemischen Industrie
  • Deutsche Forschungsgemeinschaft. Grant Numbers: BA 1821/5-2,, SCHM 444/17-2

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