The Structure of RdDddP from Roseobacter denitrificans Reveals That DMSP Lyases in the DddP-Family Are Metalloenzymes
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Hehemann-2014-The structure of RdD.pdf
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Author(s)
Hehemann, Jan-Hendrik
Law, Adrienne
Redecke, Lars
Boraston, Alisdair B.
Date Issued
July 2014
Journal
PLoS ONE
Publisher
Public Library of Science
Citation
Hehemann, Jan-Hendrik, Adrienne Law, Lars Redecke, and Alisdair B. Boraston. “The Structure of RdDddP from Roseobacter Denitrificans Reveals That DMSP Lyases in the DddP-Family Are Metalloenzymes.” Edited by Fanis Missirlis. PLoS ONE 9, no. 7 (July 23, 2014): e103128.
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Final published version
Abstract
Marine microbes degrade dimethylsulfoniopropionate (DMSP), which is produced in large quantities by marine algae and plants, with DMSP lyases into acrylate and the gas dimethyl sulfide (DMS). Approximately 10% of the DMS vents from the sea into the atmosphere and this emission returns sulfur, which arrives in the sea through rivers and runoff, back to terrestrial systems via clouds and rain. Despite their key role in this sulfur cycle DMSP lyases are poorly understood at the molecular level. Here we report the first X-ray crystal structure of the putative DMSP lyase RdDddP from Roseobacter denitrificans, which belongs to the abundant DddP family. This structure, determined to 2.15 Å resolution, shows that RdDddP is a homodimeric metalloprotein with a binuclear center of two metal ions located 2.7 Å apart in the active site of the enzyme. Consistent with the crystallographic data, inductively coupled plasma mass spectrometry (ICP-MS) and total reflection X-ray fluorescence (TRXF) revealed the bound metal species to be primarily iron. A 3D structure guided analysis of environmental DddP lyase sequences elucidated the critical residues for metal binding are invariant, suggesting all proteins in the DddP family are metalloenzymes.
MIT Department
Massachusetts Institute of Technology. Department of Civil and Environmental Engineering
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DOI of Published Version
https://doi.org/10.1371/journal.pone.0103128
