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2c4u

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Categories: Adenosyl-fluoride synthase | Single protein | Streptomyces cattleya | Delaurentis, W. | Deng, H. | Hagan, D.O. | Mcewan, A.R. | Mcglinchey, R.P. | Naismith, J.H. | Robinson, D.A. | GOL | 5'-fluorodeoxyadanosine synthase | Apo | Fda | Fluorinase | Sam | Transferase


2c4u, resolution 2.50Å

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CRYSTAL STRUCTURE OF THE APO FORM OF THE 5'-FLUORO-5'-DEOXYADENOSINE SYNTHASE ENZYME FROM STREPTOMYCES CATTLEYA

Overview

The fluorinase enzyme from Streptomyces cattleya displays an unusual, ability in biocatalysis in that it forms a C-F bond. We now report that, the enzyme will accept 2'-deoxyadenosine in place of adenosine substrates, and structural evidence reveals a reorganisation in hydrogen bonding to, accommodate this substrate series. It emerges from this study that the, enzyme does not require a planar ribose conformation of the substrate to, catalyse C-F bond formation.

About this Structure

2C4U is a Single protein structure of sequence from Streptomyces cattleya with GOL as ligand. Active as Adenosyl-fluoride synthase, with EC number 2.5.1.63 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates., Cobb SL, Deng H, McEwan AR, Naismith JH, O'Hagan D, Robinson DA, Org Biomol Chem. 2006 Apr 21;4(8):1458-60. Epub 2006 Mar 8. PMID:16604208

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