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The ACL enzyme from Clostridium propionicum catalyzes the deamination of -alanyl-CoA to form acrylyl-CoA, a reaction involved in the degradation of -alanine in this organism. Since this reaction is fully reversible, it is also of interest for the biosynthesis of ß-alanine and represents an example of the formation of an amino-acyl-CoA derivative [1]. In order to gain an insight into the mechanism of the reaction catalyzed by the enzyme structural studies were instigated. The crystal structure of the ACL protein was determined by multiple-wavelength anomalous dispersion collecting three data sets close to the zinc edge. The protein consists of 144 residues and contains one zinc atom per molecule, which was introduced during protein crystallization. Fortunately, crystals diffracted to ultra-high resolution and a high, medium and low resolution data set was recorded resulting in a very complete data set at 0.97Å resolution. The position of the zinc atom was unambiguously determined and used for initial phasing with SHELXE [2]. Automated model building was performed with ARP/wARP [3] and resulted in 139 out of 144 residues. The structure is being refined with SHELXL [4] with current refinement statistics of R=15.8% and Rfree=17.5%. The protein consists of a five-stranded anti-parallel -sheet with a long -helix lying across and shows a high structural similarity to 4-hydroxybenzoyl CoA thioesterase ( PDB code 1bvq) [5].

Ultra-high resolution structure of a β-alanyl-CoA ammonia lyase (ACL)