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8 results on '"Ogrissek, Patrick"'

3. Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage

Author

Liaci, A Manuel, Steigenberger, Barbara, Telles de Souza, Paulo Cesar, Tamara, Sem, Gröllers-Mulderij, Mariska, Ogrissek, Patrick, Marrink, Siewert J, Scheltema, Richard A, Förster, Friedrich, Liaci, A Manuel, Steigenberger, Barbara, Telles de Souza, Paulo Cesar, Tamara, Sem, Gröllers-Mulderij, Mariska, Ogrissek, Patrick, Marrink, Siewert J, Scheltema, Richard A, and Förster, Friedrich

Abstract

The signal peptidase complex (SPC) is an essential membrane complex in the endoplasmic reticulum (ER), where it removes signal peptides (SPs) from a large variety of secretory pre-proteins with exquisite specificity. Although the determinants of this process have been established empirically, the molecular details of SP recognition and removal remain elusive. Here, we show that the human SPC exists in two functional paralogs with distinct proteolytic subunits. We determined the atomic structures of both paralogs using electron cryo-microscopy and structural proteomics. The active site is formed by a catalytic triad and abuts the ER membrane, where a transmembrane window collectively formed by all subunits locally thins the bilayer. Molecular dynamics simulations indicate that this unique architecture generates specificity for SPs based on the length of their hydrophobic segments.

Published
2021

4. Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage

Author

Sub Structural Biochemistry, Afd Biomol.Mass Spect. and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Biomolecular Mass Spectrometry and Proteomics, Liaci, A Manuel, Steigenberger, Barbara, Telles de Souza, Paulo Cesar, Tamara, Sem, Gröllers-Mulderij, Mariska, Ogrissek, Patrick, Marrink, Siewert J, Scheltema, Richard A, Förster, Friedrich, Sub Structural Biochemistry, Afd Biomol.Mass Spect. and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Biomolecular Mass Spectrometry and Proteomics, Liaci, A Manuel, Steigenberger, Barbara, Telles de Souza, Paulo Cesar, Tamara, Sem, Gröllers-Mulderij, Mariska, Ogrissek, Patrick, Marrink, Siewert J, Scheltema, Richard A, and Förster, Friedrich

Published
2021

8. Norovirus–glycan interactions — how strong are they really?

Author

Peters, Thomas, Creutznacher, Robert, Maass, Thorben, Mallagaray, Alvaro, Ogrissek, Patrick, Taube, Stefan, Thiede, Lars, and Uetrecht, Charlotte

Subjects
BLOOD group antigens, NUCLEAR magnetic resonance, NUCLEAR magnetic resonance spectroscopy, MASS spectrometry, GLYCANS
Abstract

Infection with human noroviruses requires attachment to histo blood group antigens (HBGAs) via the major capsid protein VP1 as a primary step. Several crystal structures of VP1 protruding domain dimers, so called P-dimers, complexed with different HBGAs have been solved to atomic resolution. Corresponding binding affinities have been determined for HBGAs and other glycans exploiting different biophysical techniques, with mass spectrometry (MS) and nuclear magnetic resonance (NMR) spectroscopy being most widely used. However, reported binding affinities are inconsistent. At the extreme, for the same system MS detects binding whereas NMR spectroscopy does not, suggesting a fundamental source of error. In this short essay, we will explain the reason for the observed differences and compile reliable and reproducible binding affinities. We will then highlight how a combination of MS techniques and NMR experiments affords unique insights into the process of HBGA binding by norovirus capsid proteins. [ABSTRACT FROM AUTHOR]

Published
2022
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