2FSU

Crystal Structure of the PhnH Protein from Escherichia Coli

Summary for 2FSU

• Entry DOI: 10.2210/pdb2fsu/pdb
• Descriptor: Protein phnH, SODIUM ION, ACETATE ION, ... (4 entities in total)
• Functional Keywords: c-p lyase, phnh, phosphonate metabolism, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, unknown function
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 23262.39

Authors

Adams, M.A.,Luo, Y.,Zechel, D.L.,Jia, Z.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2006-01-23, release date: 2007-03-27, Last modification date: 2024-10-30)

Primary citation

Adams, M.A.,Luo, Y.,Hove-Jensen, B.,He, S.M.,van Staalduinen, L.M.,Zechel, D.L.,Jia, Z.
Crystal structure of PhnH: an essential component of carbon-phosphorus lyase in Escherichia coli.
J.Bacteriol., 190:1072-1083, 2008

PubMed Abstract: Organophosphonates are reduced forms of phosphorous that are characterized by the presence of a stable carbon-phosphorus (C-P) bond, which resists chemical hydrolysis, thermal decomposition, and photolysis. The chemically inert nature of the C-P bond has raised environmental concerns as toxic phosphonates accumulate in a number of ecosystems. Carbon-phosphorous lyase (CP lyase) is a multienzyme pathway encoded by the phn operon in gram-negative bacteria. In Escherichia coli 14 cistrons comprise the operon (phnCDEFGHIJKLMNOP) and collectively allow the internalization and degradation of phosphonates. Here we report the X-ray crystal structure of the PhnH component at 1.77 A resolution. The protein exhibits a novel fold, although local similarities with the pyridoxal 5'-phosphate-dependent transferase family of proteins are apparent. PhnH forms a dimer in solution and in the crystal structure, the interface of which is implicated in creating a potential ligand binding pocket. Our studies further suggest that PhnH may be capable of binding negatively charged cyclic compounds through interaction with strictly conserved residues. Finally, we show that PhnH is essential for C-P bond cleavage in the CP lyase pathway.

PubMed: 17993513
DOI: 10.1128/JB.01274-07

Experimental method

X-RAY DIFFRACTION (1.7 Å)