Journal
ACS CHEMICAL BIOLOGY
Volume 12, Issue 7, Pages 1919-1927Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.7b00304
Keywords
-
Categories
Funding
- Academy of Finland [256937, 263931]
- IV4SP project (Academy of Finland) [272598]
- European Community's Seventh Framework Programme under BioStruct-X [283570]
- Academy of Finland (AKA) [272598, 256937, 272598, 263931, 256937, 263931] Funding Source: Academy of Finland (AKA)
Ask authors/readers for more resources
We present a novel crystal structure of the IlvD/EDD family enzyme, L-arabinonate dehydratase from Rhizobium leguminosarum bv. trifolii (RlArDHT, EC 4.2.1.25), which catalyzes the conversion of L-arabinonate to 2-dehydro-3-deoxy-L-arabinonate. The enzyme is a tetramer consisting of a dimer of dimers, where each monomer is composed of two domains. The active site contains a catalytically important [2Fe-2S] cluster and Mg2+ ion and is buried between two domains, and also at the dimer interface. The active site Lys129 was found to be carbamylated. Ser480 and Thr482 were shown to be essential residues for catalysis, and the S480A mutant structure showed an unexpected open conformation in which the active site was more accessible for the substrate. This structure showed the partial binding of L-arabinonate, which allowed us to suggest that the alkoxide ion form of the Ser480 side chain functions as a base and the [2Fe-2S] cluster functions as a Lewis acid in the elimination reaction.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available