1MFZ

Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa

1MFZ の概要

• エントリーDOI: 10.2210/pdb1mfz/pdb
• 分子名称: GDP-mannose 6-dehydrogenase, GUANOSINE 5'-(TRIHYDROGEN DIPHOSPHATE), P'-D-MANNOPYRANOSYL ESTER (3 entities in total)
• 機能のキーワード: rossmann fold, domain-swapped dimer, enzyme complex with cofactor and product, oxidoreductase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 194791.18

構造登録者

Snook, C.F.,Tipton, P.A.,Beamer, L.J. (登録日: 2002-08-14, 公開日: 2003-05-06, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.8 Å)