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Department of Energy, Office of Science, Office of Basic Energy Sciences","award":["W-31-109-Eng-38"],"award-info":[{"award-number":["W-31-109-Eng-38"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2012,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Dimethylsulfoniopropionate (DMSP) is a ubiquitous algal metabolite and common carbon and sulfur source for marine bacteria. DMSP is a precursor for the climatically active gas dimethylsulfide that is readily oxidized to sulfate, sulfur dioxide, methanesulfonic acid, and other products that act as cloud condensation nuclei. Although the environmental importance of DMSP metabolism has been known for some time, the enzyme responsible for DMSP demethylation by marine bacterioplankton, dimethylsufoniopropionate\u2010dependent demethylase A (DmdA, EC 2.1.1.B5), has only recently been identified and biochemically characterized. In this work, we report the structure for the apoenzyme DmdA from <jats:italic>Pelagibacter ubique<\/jats:italic> (2.1 \u00c5), as well as for DmdA co\u2010crystals soaked with substrate DMSP (1.6 \u00c5) or the cofactor tetrahydrofolate (THF) (1.6 \u00c5). Surprisingly, the overall fold of the DmdA is not similar to other enzymes that typically utilize the reduced form of THF and in fact is a triple domain structure similar to what has been observed for the glycine cleavage T protein or sarcosine oxidase. Specifically, while the THF binding fold appears conserved, previous biochemical studies have shown that all enzymes with a similar fold produce 5,10\u2010methylene\u2010THF, while DmdA catalyzes a redox\u2010neutral methyl transfer reaction to produce 5\u2010methyl\u2010THF. On the basis of the findings presented herein and the available biochemical data, we outline a mechanism for a redox\u2010neutral methyl transfer reaction that is novel to this conserved THF binding domain.<\/jats:p>","DOI":"10.1002\/pro.2015","type":"journal-article","created":{"date-parts":[[2011,12,7]],"date-time":"2011-12-07T21:29:37Z","timestamp":1323293377000},"page":"289-298","source":"Crossref","is-referenced-by-count":28,"title":["Structures of dimethylsulfoniopropionate\u2010dependent demethylase from the marine organism <i>Pelagabacter ubique<\/i>"],"prefix":"10.1002","volume":"21","author":[{"given":"David J.","family":"Schuller","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chris R.","family":"Reisch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mary Ann","family":"Moran","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William B.","family":"Whitman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William N.","family":"Lanzilotta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2012,1,4]]},"reference":[{"key":"e_1_2_5_2_2","doi-asserted-by":"publisher","DOI":"10.3354\/ame024225"},{"key":"e_1_2_5_3_2","doi-asserted-by":"publisher","DOI":"10.4319\/lo.2002.47.1.0053"},{"key":"e_1_2_5_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/43168"},{"key":"e_1_2_5_5_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature00851"},{"key":"e_1_2_5_6_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature10078"},{"key":"e_1_2_5_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00770-08"},{"key":"e_1_2_5_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0169-5347(01)02152-8"},{"key":"e_1_2_5_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.65.10.4549-4558.1999"},{"key":"e_1_2_5_10_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.221.4612.744"},{"key":"e_1_2_5_11_2","doi-asserted-by":"crossref","first-page":"3292","DOI":"10.1128\/aem.56.11.3292-3297.1990","article-title":"Dimethyl sulfide production from dimethylsulfoniopropionate in coastal seawater samples and bacterial cultures","volume":"56","author":"Kiene RP","year":"1990","journal-title":"Appl Environ Microbiol"},{"key":"e_1_2_5_12_2","doi-asserted-by":"publisher","DOI":"10.1038\/326655a0"},{"key":"e_1_2_5_13_2","doi-asserted-by":"publisher","DOI":"10.1038\/237452a0"},{"key":"e_1_2_5_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/0304-4203(96)00006-0"},{"key":"e_1_2_5_15_2","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/cdg395"},{"key":"e_1_2_5_16_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M409672200"},{"key":"e_1_2_5_17_2","doi-asserted-by":"publisher","DOI":"10.2116\/analsci.17.565"},{"key":"e_1_2_5_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(99)80043-4"},{"key":"e_1_2_5_19_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj2030707"},{"key":"e_1_2_5_20_2","first-page":"71","article-title":"Glycine metabolism by rat liver mitochondria. 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