1FWR

CRYSTAL STRUCTURE OF KDPG ALDOLASE DOUBLE MUTANT K133Q/T161K

Summary for 1FWR

• Entry DOI: 10.2210/pdb1fwr/pdb
• Related: 1FQ0
• Descriptor: KDPG ALDOLASE, CITRIC ACID (3 entities in total)
• Functional Keywords: tim barrel, lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 3
• Total formula weight: 67572.30

Authors

Naismith, J.H.,Buchanan, L.V. (deposition date: 2000-09-24, release date: 2000-10-04, Last modification date: 2024-02-07)

Primary citation

Wymer, N.,Buchanan, L.V.,Henderson, D.,Mehta, N.,Botting, C.H.,Pocivavsek, L.,Fierke, C.A.,Toone, E.J.,Naismith, J.H.
Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli.
Structure, 9:1-10, 2001

PubMed Abstract: Aldolases are carbon bond-forming enzymes that have long been identified as useful tools for the organic chemist. However, their utility is limited in part by their narrow substrate utilization. Site-directed mutagenesis of various enzymes to alter their specificity has been performed for many years, typically without the desired effect. More recently directed evolution has been employed to engineer new activities onto existing scaffoldings. This approach allows random mutation of the gene and then selects for fitness to purpose those proteins with the desired activity. To date such approaches have furnished novel activities through multiple mutations of residues involved in recognition; in no instance has a key catalytic residue been altered while activity is retained.

PubMed: 11342129
DOI: 10.1016/S0969-2126(00)00555-4

Experimental method

X-RAY DIFFRACTION (2.7 Å)