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3fua
From Proteopedia
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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 [L-fuculose-phosphate aldolase], with EC number [4.1.2.17]. Structure known Active Sites: ACT and PBS. 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 Tue Oct 30 17:45:17 2007
Categories: Escherichia coli | L-fuculose-phosphate aldolase | Single protein | Dreyer, M.K. | Schulz, G.E. | BME | CL | SO4 | ZN | Class ii aldolase | Lyase | Zinc enzyme
