1G58

CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE GOLD DERIVATIVE

Summary for 1G58

• Entry DOI: 10.2210/pdb1g58/pdb
• Descriptor: 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE, GOLD ION (3 entities in total)
• Functional Keywords: dihydroxybutanone phosphate synthase, riboflavin biosynthesis, skeletal rearrangement, antimicrobial target, structure-based design, isomerase
• Biological source: Escherichia coli
• Cellular location: Cell membrane; Peripheral membrane protein (Potential): P0A7J0
• Total number of polymer chains: 2
• Total formula weight: 47064.81

Authors

Liao, D.-I.,Calabrese, J.C.,Wawrzak, Z.,Viitanen, P.V.,Jordan, D.B. (deposition date: 2000-10-30, release date: 2001-04-30, Last modification date: 2024-02-07)

Primary citation

Liao, D.I.,Calabrese, J.C.,Wawrzak, Z.,Viitanen, P.V.,Jordan, D.B.
Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis.
Structure, 9:11-18, 2001

PubMed Abstract: 3,4-Dihydroxy-2-butanone-4-phosphate synthase catalyzes a commitment step in the biosynthesis of riboflavin. On the enzyme, ribulose 5-phosphate is converted to 3,4-dihydroxy-2-butanone 4-phosphate and formate in steps involving enolization, ketonization, dehydration, skeleton rearrangement, and formate elimination. The enzyme is absent in humans and an attractive target for the discovery of antimicrobials for pathogens incapable of acquiring sufficient riboflavin from their hosts. The homodimer of 23 kDa subunits requires Mg(2+) for activity.

PubMed: 11342130
DOI: 10.1016/S0969-2126(00)00550-5

Experimental method

X-RAY DIFFRACTION (1.55 Å)