1MUU

Crystal structure of GDP-mannose dehydrogenase: A key enzyme of alginate biosynthesis in P. aeruginosa

(2003) Biochemistry 42: 4658-4668

• PubMed: 12705829 Search on PubMed
• DOI: https://doi.org/10.1021/bi027328k
• Primary Citation of Related Structures:  
  1MFZ, 1MUU, 1MV8


• 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.

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Organizational Affiliation: 

Department of Biochemistry, 117 Schweitzer Hall, University of Missouri-Columbia, Columbia, Missouri 65211, USA.