Chemical shift assignments of domain 4 from the phosphohexomutase from Pseudomonas aeruginosa suggest that freeing perturbs its coevolved domain interface

Biomol NMR Assign. 2014 Oct;8(2):329-33. doi: 10.1007/s12104-013-9511-5. Epub 2013 Jul 28.

Abstract

A domain needed for the catalytic efficiency of an enzyme model of simple processivity and domain-domain interactions has been characterized by NMR. This domain 4 from phosphomannomutase/phosphoglucomutase (PMM/PGM) closes upon glucose phosphate and mannose phosphate ligands in the active site, and can modestly reconstitute activity of enzyme truncated to domains 1-3. This enzyme supports biosynthesis of the saccharide-derived virulence factors (rhamnolipids, lipopolysaccharides, and alginate) of the opportunistic bacterial pathogen Pseudomonas aeruginosa. (1)H, (13)C, and (15)N NMR chemical shift assignments of domain 4 of PMM/PGM suggest preservation and independence of its structure when separated from domains 1-3. The face of domain 4 that packs with domain 3 is perturbed in NMR spectra without disrupting this fold. The perturbed residues overlap both the most highly coevolved positions in the interface and residues lining a cavity at the domain interface.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Evolution, Molecular*
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular*
  • Phosphoglucomutase / chemistry*
  • Phosphoglucomutase / metabolism*
  • Phosphotransferases (Phosphomutases) / chemistry*
  • Phosphotransferases (Phosphomutases) / metabolism*
  • Protein Structure, Tertiary
  • Pseudomonas aeruginosa / enzymology*

Substances

  • Phosphotransferases (Phosphomutases)
  • Phosphoglucomutase
  • phosphomannomutase