Improving integrative 3D modeling into low- to medium-resolution electron microscopy structures with evolutionary couplings.

ABSTRACT: Electron microscopy (EM) continues to provide near-atomic resolution structures for well-behaved proteins and protein complexes. Unfortunately, structures of some complexes are limited to low- to medium-resolution due to biochemical or conformational heterogeneity. Thus, the application of unbiased systematic methods for fitting individual structures into EM maps is important. A method that employs co-evolutionary information obtained solely from sequence data could prove invaluable for quick, confident localization of subunits within these structures. Here, we incorporate the co-evolution of intermolecular amino acids as a new type of distance restraint in the integrative modeling platform in order to build three-dimensional models of atomic structures into EM maps ranging from 10-14 Å in

SUBMITTER: McCafferty CL 

PROVIDER: S-EPMC8040867 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature