A hybrid NMR/SAXS‐based approach for discriminating oligomeric protein interfaces using Rosetta
Abstract
Oligomeric proteins are important targets for structure determination in solution. While in most cases the fold of individual subunits can be determined experimentally, or predicted by homology‐based methods, protein–protein interfaces are challenging to determine de novo using conventional NMR structure determination protocols. Here we focus on a member of the bet‐V1 superfamily, Aha1 from Colwellia psychrerythraea. This family displays a broad range of crystallographic interfaces none of which can be reconciled with the NMR and SAXS data collected for Aha1. Unlike conventional methods relying on a dense network of experimental restraints, the sparse data are used to limit conformational search during optimization of a physically realistic energy function. This work highlights a new approach for studying minor conformational changes due to structural plasticity within a single dimeric interface in solution. Proteins 2015; 83:309–317. © 2014 Wiley Periodicals, Inc.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Dec 19, 2014
- Source ID
- 10.1002/prot.24719
Entities
People
- Christopher M. Barbieri
- David Baker
- Edward H. Snell
- Gaetano T. Montelione
- Gaohua Liu
- Hsiau‐wei Lee
- Joseph R. Luft
- Lei Shi
- Nikolaos G. Sgourakis
- Oliver F. Lange
- Paolo Rossi
- R. F. Xiao
- Thomas B. Acton
- Thomas D. Grant
Organizations
- Defense Threat Reduction Agency
- Hauptman-Woodward Medical Research Institute
- Howard Hughes Medical Institute
- National Institute of Diabetes and Digestive and Kidney Diseases
- National Institute of General Medical Sciences
- National Institutes of Health
- Robert Wood Johnson Medical School
- Rutgers University
- University at Buffalo
- University of Georgia
- University of Washington
- Yusuf Hamied Department of Chemistry