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

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

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

Content Provider	PubMed Central
Author	Wei, Yirui Marcink, Thomas C. Jia, Xu Sirianni, Arthur G. Sarma, Akella V. S. Prior, Stephen H. Beamer, Lesa J. Doren, Steven R. Van
Copyright Year	2013
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, lipo-polysaccharides, and alginate) of the opportunistic bacterial pathogen Pseudomonas aeruginosa. 1H, 13C, and 15N 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.
Related Links	http://dx.doi.org/10.1007/s12104-013-9511-5
Ending Page	333
Page Count	5
Starting Page	329
File Format	PDF
ISSN	18742718
e-ISSN	1874270X
Journal	Biomolecular NMR assignments
Issue Number	2
Volume Number	8
Language	English
Publisher Date	2014-10-01
Access Restriction	Open
Subject Keyword	Biochemistry Structural Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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

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

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

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