Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer

Riyaz Maderbocus, Blanche L. Fields, Keith Hamilton, Shukun Luo, Timothy H. Tran, Lars E. P. Dietrich and Liang Tong ()
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Riyaz Maderbocus: Columbia University
Blanche L. Fields: Columbia University
Keith Hamilton: Columbia University
Shukun Luo: Columbia University
Timothy H. Tran: Columbia University
Lars E. P. Dietrich: Columbia University
Liang Tong: Columbia University

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: Abstract Pseudomonas species and other aerobic bacteria have a biotin-independent malonate decarboxylase that is crucial for their utilization of malonate as the sole carbon and energy source. The malonate decarboxylase holoenzyme contains four subunits, having an acyl-carrier protein (MdcC subunit) with a distinct prosthetic group, as well as decarboxylase (MdcD–MdcE) and acyl-carrier protein transferase (MdcA) catalytic activities. Here we report the crystal structure of a Pseudomonas malonate decarboxylase hetero-tetramer, as well as biochemical and functional studies based on the structural information. We observe a malonate molecule in the active site of MdcA and we also determine the structure of malonate decarboxylase with CoA in the active site of MdcD–MdcE. Both structures provide molecular insights into malonate decarboxylase catalysis. Mutations in the hetero-tetramer interface can abolish holoenzyme formation. Mutations in the hetero-tetramer interface and the active sites can abolish Pseudomonas aeruginosa growth in a defined medium with malonate as the sole carbon source.

Date: 2017
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DOI: 10.1038/s41467-017-00233-z

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