title: Chemical shift assignments of domain 4 from the phosphohexomutase from Pseudomonas aeruginosa suggest that freeing perturbs its coevolved domain interface.
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.
authors.affiliation: Biochemistry Department, University of Missouri, 117 Schweitzer Hall, Columbia, MO, 65211, USA.
authors.forename: Yirui
authors.initials: Y
authors.lastname: Wei
authors.forename: Thomas C
authors.initials: TC
authors.lastname: Marcink
authors.forename: Jia
authors.initials: J
authors.lastname: Xu
authors.forename: Arthur G
authors.initials: AG
authors.lastname: Sirianni
authors.forename: Akella V S
authors.initials: AV
authors.lastname: Sarma
authors.forename: Stephen H
authors.initials: SH
authors.lastname: Prior
authors.forename: Lesa J
authors.initials: LJ
authors.lastname: Beamer
authors.forename: Steven R
authors.initials: SR
authors.lastname: Van Doren
mesh_terms: D019143:Evolution, Molecular; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010733:Phosphoglucomutase / Q000737:chemistry* / Q000378:metabolism*; D017875:Phosphotransferases (Phosphomutases) / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011550:Pseudomonas aeruginosa / Q000201:enzymology*
chemical_list: D017875:Phosphotransferases (Phosphomutases); D010733:Phosphoglucomutase; C052799:phosphomannomutase
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