1MFZ
Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa
Summary for 1MFZ
| Entry DOI | 10.2210/pdb1mfz/pdb |
| Descriptor | GDP-mannose 6-dehydrogenase, GUANOSINE 5'-(TRIHYDROGEN DIPHOSPHATE), P'-D-MANNOPYRANOSYL ESTER (3 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 | 194791.18 |
| Authors | Snook, C.F.,Tipton, P.A.,Beamer, L.J. (deposition date: 2002-08-14, release date: 2003-05-06, Last modification date: 2024-10-16) |
| 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 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 (2.8 Å) |
Structure validation
Download full validation report
