Crystal Structure of the Carbon-Phosphorus Lyase Complex from Escherichia coli

• Published in: Acta crystallographica. Section A, Foundations and advances Foundations and advances, 2014-08, Vol.70 (a1), p.C1060-C1060
• Main Authors: Seweryn, Paulina, Van, Lan, Kjeldgaard, Morten, Hove-Jensen, Bjarne, Jochimsen, Bjarne, Brodersen, Ditlev
• Format: Article
• Language: English
• ISSN: 2053-2733; 2053-2733
• DOI: 10.1107/S2053273314089396

Abstract only Phosphorus is an essential element for all living cells and is usually taken up in the form of phosphate. A number of microorganisms, however, are capable of extracting phosphorous from organic phosphonate compounds, which are characterized by a stable carbon-phosphorus (C-P) bond (1). The metabolic pathway responsible for phosphonate degradation is still poorly understood, but the process is known to involve two reactions before the actual C-P bond cleavage, which has been proposed to take place via a radical mechanism. A key component in the process is C-P lyase, an enzyme encoded by phnJ within the phn operon (2). To get a better insight into the mechanism of this complex degradation pathway, we have determined the crystal structure of the core of a multi-subunit enzymatic complex including the C-P lyase component with a total molecular mass of 220 kDa (3). The structure reveals the overall architecture of the C-P lyase and has important implications for our understanding of enzyme mechanism and catalysis.