1e4a
L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT DEL(27)
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OverviewOverview
The crystal structures of l-fuculose-1-phosphate aldolase (FucA) with and, without a ligated analogue of dihydroxyacetone phosphate (DHAP) and of a, number of active center mutants have resulted in a model of the catalytic, mechanism. This model has now been confirmed by structural analyses of, further mutations at the zinc coordination sphere and at the phosphate, site. In addition, these mutants have revealed new aspects of the, catalysis: the hydroxyl group of Tyr113' (from a neighboring subunit), which sits just outside the zinc coordination sphere, steers DHAP towards, a productive binding mode at the zinc ion; Glu73 contacts zinc in between, the two ligand positions intended for the DHAP oxygen atoms and thus, avoids blocking of these positions by a tetrahedrally coordinated ... [(full description)]
About this StructureAbout this Structure
1E4A is a [Single protein] structure of sequence from [Escherichia coli] with SO4, ZN and BME as [ligands]. Active as [L-fuculose-phosphate aldolase], with EC number [4.1.2.17]. Structure known Active Sites: ACT and MUT. Full crystallographic information is available from [OCA].
ReferenceReference
Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis., Joerger AC, Mueller-Dieckmann C, Schulz GE, J Mol Biol. 2000 Nov 3;303(4):531-43. PMID:11054289
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