1MV8

1.55 A crystal structure of a ternary complex of GDP-mannose dehydrogenase from Psuedomonas aeruginosa

Summary for 1MV8

• Entry DOI: 10.2210/pdb1mv8/pdb
• Related: 1MF2 1MUU
• Related PRD ID: PRD_900003
• Descriptor: GDP-mannose 6-dehydrogenase, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (7 entities in total)
• Functional Keywords: rossmann fold, domain-swapped dimer, enzyme complex with cofactor and product, oxidoreductase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 4
• Total formula weight: 196679.56

Authors

Snook, C.F.,Tipton, P.A.,Beamer, L.J. (deposition date: 2002-09-24, release date: 2003-05-06, Last modification date: 2024-02-14)

Primary citation

Snook, C.F.,Tipton, P.A.,Beamer, L.J.
The crystal structure of GDP-mannose dehydrogenase: A key enzyme in alginate biosynthesis of P. aeruginosa
Biochemistry, 42:4658-4668, 2003

PubMed Abstract: The enzyme GMD from Pseudomonas aeruginosa catalyzes the committed step in the synthesis of the exopolysaccharide alginate. Alginate is a major component of P. aeruginosa biofilms that protect the bacteria from the host immune response and antibiotic therapy. The 1.55 A crystal structure of GMD in ternary complex with its cofactor NAD(H) and product GDP-mannuronic acid reveals that the enzyme forms a domain-swapped dimer with two polypeptide chains contributing to each active site. The extensive dimer interface provides multiple opportunities for intersubunit communication. Comparison of the GMD structure with that of UDP-glucose dehydrogenase reveals the structural basis of sugar binding specificity that distinguishes these two related enzyme families. The high-resolution structure of GMD provides detailed information on the active site of the enzyme and a template for structure-based inhibitor design.

PubMed: 12705829
DOI: 10.1021/bi027328k

Experimental method

X-RAY DIFFRACTION (1.55 Å)