PELDOR spectroscopy distance fingerprinting of the octameric outer-membrane protein Wza from Escherichia coli

Angew Chem Int Ed Engl. 2009;48(16):2904-6. doi: 10.1002/anie.200805758.

Abstract

Distance fingerprinting: Pulsed electron-electron double resonance spectroscopy (PELDOR) is applied to the octameric membrane protein complex Wza of E. coli. The data yielded a detailed distance fingerprint of its periplasmic region that compares favorably to the crystal structure. These results provide the foundation to study conformation changes from interaction with partner proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Bacterial Outer Membrane Proteins / chemistry*
  • Computer Simulation
  • Crystallography, X-Ray
  • Electron Spin Resonance Spectroscopy
  • Escherichia coli / chemistry*
  • Escherichia coli Proteins / chemistry*
  • Mutant Proteins / chemistry
  • Periplasm / metabolism
  • Protein Structure, Tertiary

Substances

  • Bacterial Outer Membrane Proteins
  • Escherichia coli Proteins
  • Mutant Proteins
  • Wza protein, E coli