This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3fua
From Proteopedia
|
L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K
Overview
The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form, has been determined with and without the inhibitor, phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm), resolution, respectively. This inhibitor mimics the enediolate transition, state of the substrate moiety dihydroxyacetone phosphate. The structures, showed that dihydroxyacetone phosphate ligates the zinc ion of this, metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar, environment. At this position Glu73 accepts a proton in the initial, reaction step, producing the enediolate which is then stabilized by the, zinc ion. The other substrate moiety L-lactaldehyde was modeled, because, no binding structure ... [(full description)]
About this Structure
3FUA is a [Single protein] structure of sequence from [Escherichia coli] with ZN, SO4, CL and BME as [ligands]. Active as [[1]], with EC number [4.1.2.17]. Full crystallographic information is available from [OCA].
Reference
Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure., Dreyer MK, Schulz GE, J Mol Biol. 1996 Jun 14;259(3):458-66. PMID:8676381
Page seeded by OCA on Mon Oct 29 20:59:20 2007
Categories: Escherichia coli | Single protein | Dreyer, M.K. | Schulz, G.E. | BME | CL | SO4 | ZN | Class ii aldolase | Lyase | Zinc enzyme
