1MUU
2.0 A crystal structure of GDP-mannose dehydrogenase
Summary for 1MUU
| Entry DOI | 10.2210/pdb1muu/pdb |
| Related PRD ID | PRD_900003 |
| Descriptor | GDP-mannose 6-dehydrogenase, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 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 | 197787.17 |
| Authors | Snook, C.F.,Tipton, P.A.,Beamer, L.J. (deposition date: 2002-09-24, release date: 2003-05-06, Last modification date: 2024-10-30) |
| Primary citation | Snook, C.F.,Tipton, P.A.,Beamer, L.J. Crystal structure of GDP-mannose dehydrogenase: A key enzyme of alginate biosynthesis in P. aeruginosa Biochemistry, 42:4658-4668, 2003 Cited by 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: 12705829DOI: 10.1021/bi027328k PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
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