{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,25]],"date-time":"2026-10-25T02:30:04Z","timestamp":1792895404917,"version":"4.5.0"},"reference-count":31,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[2008,2,1]],"date-time":"2008-02-01T00:00:00Z","timestamp":1201824000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2008,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            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\n            <jats:italic>phn<\/jats:italic>\n            operon in gram-negative bacteria. In\n            <jats:italic>Escherichia coli<\/jats:italic>\n            14 cistrons comprise the operon (\n            <jats:italic>phnCDEFGHIJKLMNOP<\/jats:italic>\n            ) 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\u030a resolution. The protein exhibits a novel fold, although local similarities with the pyridoxal 5\u2032-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.\n          <\/jats:p>","DOI":"10.1128\/jb.01274-07","type":"journal-article","created":{"date-parts":[[2007,11,10]],"date-time":"2007-11-10T01:25:33Z","timestamp":1194657933000},"page":"1072-1083","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":40,"title":["Crystal Structure of PhnH: an Essential Component of Carbon-Phosphorus Lyase in\n            <i>Escherichia coli<\/i>"],"prefix":"10.1128","volume":"190","author":[{"given":"Melanie A.","family":"Adams","sequence":"first","affiliation":[{"name":"Departments of Biochemistry"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yan","family":"Luo","sequence":"additional","affiliation":[{"name":"Chemistry, Queen's University, Kingston, Ontario, Canada K7L3N6"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bjarne","family":"Hove-Jensen","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology, University of Copenhagen, Copenhagen, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shu-Mei","family":"He","sequence":"additional","affiliation":[{"name":"Chemistry, Queen's University, Kingston, Ontario, Canada K7L3N6"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura M.","family":"van Staalduinen","sequence":"additional","affiliation":[{"name":"Departments of Biochemistry"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David L.","family":"Zechel","sequence":"additional","affiliation":[{"name":"Chemistry, Queen's University, Kingston, Ontario, Canada K7L3N6"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zongchao","family":"Jia","sequence":"additional","affiliation":[{"name":"Departments of Biochemistry"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"D226","DOI":"10.1093\/nar\/gkh039","volume":"32","year":"2004","unstructured":"Andreeva, A., D. Howorth, S. E. Brenner, T. J. Hubbard, C. Chothia, and A. G. Murzin. 2004. SCOP database in 2004: refinements integrate structure and sequence family data. Nucleic Acids Res. 32 : D226-D229.","journal-title":"Nucleic Acids Res."},{"key":"e_1_3_2_3_2","unstructured":"Reference deleted."},{"key":"e_1_3_2_4_2","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0960-894X(01)81089-1","volume":"1","year":"1991","unstructured":"Avila, L. Z., K. M. Draths, and J. W. Frost. 1991. Metabolites associated with organophosphonate C-P bond cleavage: chemical synthesis and microbial degradation of [32P]-ethylphosphonic acid. Biorg. Chem. Lett. 1 : 51-54.","journal-title":"Biorg. Chem. Lett."},{"key":"e_1_3_2_5_2","first-page":"905","volume":"54","year":"1998","unstructured":"Brunger, A. T., P. D. Adams, G. M. Clore, W. L. DeLano, P. Gros, R. W. Grosse-Kunstleve, J. S. Jiang, J. Kuszewski, M. Nilges, N. S. Pannu, R. J. Read, L. M. Rice, T. Simonson, and G. L. Warren. 1998. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. Sect. D 54 : 905-921.","journal-title":"Acta Crystallogr. Sect. D"},{"key":"e_1_3_2_6_2","unstructured":"Programs XFIT and FOURYA. 1996"},{"key":"e_1_3_2_7_2","doi-asserted-by":"crossref","first-page":"4461","DOI":"10.1016\/S0021-9258(19)39587-0","volume":"265","year":"1990","unstructured":"Chen, C. M., Q. Z. Ye, Z. M. Zhu, B. L. Wanner, and C. T. Walsh. 1990. Molecular biology of carbon-phosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B. J. Biol. Chem. 265 : 4461-4471.","journal-title":"B. J. Biol. Chem."},{"key":"e_1_3_2_8_2","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1038\/nature04203","volume":"439","year":"2006","unstructured":"Dyhrman, S. T., P. D. Chappell, S. T. Haley, J. W. Moffett, E. D. Orchard, J. B. Waterbury, and E. A. Webb. 2006. 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