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Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD

  • Michael Kovermann

    Michael Kovermann received his diploma degree in medical physics at the Martin-Luther-Universität Halle-Wittenberg, Germany, 2006. During his PhD in the biophysics lab of Jochen Balbach in the Physics Department of the same university, he focused on the NMR characterization of functional protein states. He solved several protein structures by this method and could relate protein function with protein dynamics. Currently, he is a postdoctoral fellow at the Umeå University in the group of Magnus Wolf-Watz.

         , Franz X. Schmid

    Franz-Xaver Schmid studied chemistry at the Technische Universität Berlin and the Universität Regensburg (Germany), where he received his PhD for an analysis of substrate binding to dehydrogenases in 1977. After a postdoctoral stay at Stanford with Robert L. Baldwin, he received the venia legendi for biochemistry at the Universität Regensburg in the department of Rainer Jaenicke. Since 1988, he has been professor of biochemistry at the Universität Bayreuth, where he focuses on protein folding and its catalysis by folding enzymes. He is a member of the Deutsche Nationale Akademie der Wissenschaften, Leopoldina.

         and Jochen Balbach

    Jochen Balbach studied chemistry at the Technische Universität München, where he also received his PhD for protein NMR studies in 1994. After a postdoctoral stay at the University of Oxford with Chris M. Dobson, he received the venia legendi for biochemistry at the University of Bayreuth under the supervision of Franz X. Schmid. Since 2004, he is professor of biophysics and medical physics at the Martin-Luther-Universität Halle-Wittenberg. He is interested in the structural biology and biophysics of proteins, their dynamics and folding reactions.

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Published/Copyright: March 28, 2013
Biological Chemistry
From the journal Biological Chemistry Volume 394 Issue 8

Abstract

SlyD is a bacterial two-domain protein that functions as a molecular chaperone, a prolyl cis/trans isomerase, and a nickel-binding protein. This review summarizes recent findings about the molecular enzyme mechanism of SlyD. The chaperone function located in one domain of SlyD is involved in twin-arginine translocation and increases the catalytic efficiency of the prolyl cis/trans isomerase domain in protein folding by two orders of magnitude. The C-terminal tail of SlyD binds Ni2+ ions and supplies them for the maturation of [NiFe] hydrogenases. A combined biochemical and biophysical analysis revealed the molecular basis of the delicate interplay of the different domains of SlyD for optimal function.

Keywords: chaperone; enzyme mechanism; nickel metalloprotein; protein folding; prolyl isomerase
Corresponding author: Jochen Balbach, Institut für Physik, Biophysik, und Mitteldeutsches Zentrum für Struktur und Dynamik der Proteine (MZP), Martin-Luther Universität Halle-Wittenberg, D-06120 Halle, Germany

About the authors

Michael Kovermann

Michael Kovermann received his diploma degree in medical physics at the Martin-Luther-Universität Halle-Wittenberg, Germany, 2006. During his PhD in the biophysics lab of Jochen Balbach in the Physics Department of the same university, he focused on the NMR characterization of functional protein states. He solved several protein structures by this method and could relate protein function with protein dynamics. Currently, he is a postdoctoral fellow at the Umeå University in the group of Magnus Wolf-Watz.

Franz X. Schmid

Franz-Xaver Schmid studied chemistry at the Technische Universität Berlin and the Universität Regensburg (Germany), where he received his PhD for an analysis of substrate binding to dehydrogenases in 1977. After a postdoctoral stay at Stanford with Robert L. Baldwin, he received the venia legendi for biochemistry at the Universität Regensburg in the department of Rainer Jaenicke. Since 1988, he has been professor of biochemistry at the Universität Bayreuth, where he focuses on protein folding and its catalysis by folding enzymes. He is a member of the Deutsche Nationale Akademie der Wissenschaften, Leopoldina.

Jochen Balbach

Jochen Balbach studied chemistry at the Technische Universität München, where he also received his PhD for protein NMR studies in 1994. After a postdoctoral stay at the University of Oxford with Chris M. Dobson, he received the venia legendi for biochemistry at the University of Bayreuth under the supervision of Franz X. Schmid. Since 2004, he is professor of biophysics and medical physics at the Martin-Luther-Universität Halle-Wittenberg. He is interested in the structural biology and biophysics of proteins, their dynamics and folding reactions.

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Received: 2013-1-31
Accepted: 2013-3-26
Published Online: 2013-03-28
Published in Print: 2013-08-01

©2013 by Walter de Gruyter Berlin Boston

Articles in the same Issue

  1. Masthead
  2. Masthead
  3. Guest Editorial
  4. Highlight: Protein states with cell biological and medicinal relevance
  5. HIGHLIGHT: PROTEIN STATES WITH CELL BIOLOGICAL AND MEDICAL RELEVANCE
  6. Towards improved receptor targeting: anterograde transport, internalization and postendocytic trafficking of neuropeptide Y receptors
  7. Progress in demystification of adhesion G protein-coupled receptors
  8. The unresolved puzzle why alanine extensions cause disease
  9. Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD
  10. Structure and allosteric regulation of eukaryotic 6-phosphofructokinases
  11. Polyionic and cysteine-containing fusion peptides as versatile protein tags
  12. p0071/PKP4, a multifunctional protein coordinating cell adhesion with cytoskeletal organization
  13. Lysine-specific histone demethylase LSD1 and the dynamic control of chromatin
  14. Methylation of the nuclear poly(A)-binding protein by type I protein arginine methyltransferases – how and why
  15. Oxidative in vitro folding of a cysteine deficient variant of the G protein-coupled neuropeptide Y receptor type 2 improves stability at high concentration
  16. Identification of prolyl oligopeptidase as a cyclosporine-sensitive protease by screening of mouse liver extracts
  17. In vitro maturation of Drosophila melanogaster Spätzle protein with refolded Easter reveals a novel cleavage site within the prodomain
  18. Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains
  19. High level expression of the Drosophila Toll receptor ectodomain and crystallization of its complex with the morphogen Spätzle
https://doi.org/10.1515/hsz-2013-0137
Keywords for this article
chaperone; enzyme mechanism; nickel metalloprotein; protein folding; prolyl isomerase

Articles in the same Issue

  1. Masthead
  2. Masthead
  3. Guest Editorial
  4. Highlight: Protein states with cell biological and medicinal relevance
  5. HIGHLIGHT: PROTEIN STATES WITH CELL BIOLOGICAL AND MEDICAL RELEVANCE
  6. Towards improved receptor targeting: anterograde transport, internalization and postendocytic trafficking of neuropeptide Y receptors
  7. Progress in demystification of adhesion G protein-coupled receptors
  8. The unresolved puzzle why alanine extensions cause disease
  9. Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD
  10. Structure and allosteric regulation of eukaryotic 6-phosphofructokinases
  11. Polyionic and cysteine-containing fusion peptides as versatile protein tags
  12. p0071/PKP4, a multifunctional protein coordinating cell adhesion with cytoskeletal organization
  13. Lysine-specific histone demethylase LSD1 and the dynamic control of chromatin
  14. Methylation of the nuclear poly(A)-binding protein by type I protein arginine methyltransferases – how and why
  15. Oxidative in vitro folding of a cysteine deficient variant of the G protein-coupled neuropeptide Y receptor type 2 improves stability at high concentration
  16. Identification of prolyl oligopeptidase as a cyclosporine-sensitive protease by screening of mouse liver extracts
  17. In vitro maturation of Drosophila melanogaster Spätzle protein with refolded Easter reveals a novel cleavage site within the prodomain
  18. Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains
  19. High level expression of the Drosophila Toll receptor ectodomain and crystallization of its complex with the morphogen Spätzle
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