In Situ Structural Restraints from Cross-Linking Mass Spectrometry in Human Mitochondria.

ABSTRACT: The field of structural biology is increasingly focusing on studying proteins in situ, i.e., in their greater biological context. Cross-linking mass spectrometry (CLMS) is contributing to this effort, typically through the use of mass spectrometry (MS)-cleavable cross-linkers. Here, we apply the popular noncleavable cross-linker disuccinimidyl suberate (DSS) to human mitochondria and identify 5518 distance restraints between protein residues. Each distance restraint on proteins or their interactions provides structural information within mitochondria. Comparing these restraints to protein data bank (PDB)-deposited structures and comparative models reveals novel protein conformations. Our data suggest, among others, substrates and protein flexibility of mitochondrial heat shock proteins. Th

SUBMITTER: Ryl PSJ 

PROVIDER: S-EPMC7010328 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature