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TitleStructure of the human signal peptidase complex reveals the determinants for signal peptide cleavage.
Journal, issue, pagesMol Cell, Vol. 81, Issue 19, Page 3934-3948.e11, Year 2021
Publish dateOct 7, 2021
AuthorsA Manuel Liaci / Barbara Steigenberger / Paulo Cesar Telles de Souza / Sem Tamara / Mariska Gröllers-Mulderij / Patrick Ogrissek / Siewert J Marrink / Richard A Scheltema / Friedrich Förster /
PubMed AbstractThe 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 ...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.
External linksMol Cell / PubMed:34388369
MethodsEM (single particle)
Resolution4.9 Å
Structure data

13171

7p2p

EMDB-13171, PDB-7p2p:
Human Signal Peptidase Complex Paralog A (SPC-A)
Method: EM (single particle) / Resolution: 4.9 Å

13172

7p2q

EMDB-13172, PDB-7p2q:
Human Signal Peptidase Complex Paralog C (SPC-C)
Method: EM (single particle) / Resolution: 4.9 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Endoplasmic Reticulum / Signal peptide / Serine protease / Membrane complex

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