1DB3

E.COLI GDP-MANNOSE 4,6-DEHYDRATASE

Summary for 1DB3

• Entry DOI: 10.2210/pdb1db3/pdb
• Descriptor: GDP-MANNOSE 4,6-DEHYDRATASE (2 entities in total)
• Functional Keywords: dehydratase, nadp, gdp-mannose, gdp-fucose, lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 41967.53

Authors

Somoza, J.R.,Menon, S.,Somers, W.S.,Sullivan, F.X. (deposition date: 1999-11-02, release date: 1999-11-24, Last modification date: 2024-02-07)

Primary citation

Somoza, J.R.,Menon, S.,Schmidt, H.,Joseph-McCarthy, D.,Dessen, A.,Stahl, M.L.,Somers, W.S.,Sullivan, F.X.
Structural and kinetic analysis of Escherichia coli GDP-mannose 4,6 dehydratase provides insights into the enzyme's catalytic mechanism and regulation by GDP-fucose.
Structure Fold.Des., 8:123-135, 2000

PubMed Abstract: GDP-mannose 4,6 dehydratase (GMD) catalyzes the conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose. This is the first and regulatory step in the de novo biosynthesis of GDP-(L)-fucose. Fucose forms part of a number of glycoconjugates, including the ABO blood groups and the selectin ligand sialyl Lewis X. Defects in GDP-fucose metabolism have been linked to leukocyte adhesion deficiency type II (LADII).

PubMed: 10673432
DOI: 10.1016/S0969-2126(00)00088-5

Experimental method

X-RAY DIFFRACTION (2.3 Å)