3tfh | pdb_00003tfh

DMSP-dependent demethylase from P. ubique - apo

spinqualitylabelsall models 3tfh, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tfh is a 2 chain structure with sequence from Candidatus pelagibacter ubique htcc1062. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, NA Related: 3tfi, 3tfj Gene: dmdA, SAR11_0246 (Candidatus Pelagibacter ubique HTCC1062) Activity: Aminomethyltransferase, with EC number 2.1.2.10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DMDA_PELUB] Major contributor to the demethylation of dimethlysulfonioproprionate (DMSP). Demethylates DMSP to methyl-mercaptopropionate (MMPA). Publication Abstract from PubMed 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-dependent 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 Pelagibacter ubique (2.1 A), as well as for DmdA co-crystals soaked with substrate DMSP (1.6 A) or the cofactor tetrahydrofolate (THF) (1.6 A). 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-methylene-THF, while DmdA catalyzes a redox-neutral methyl transfer reaction to produce 5-methyl-THF. Based on the findings presented herein and the available biochemical data, we outline a mechanism for a redox-neutral methyl transfer reaction that is novel to this conserved THF binding domain. Structures of dimethylsulfoniopropionate-dependent demethylase from the marine organism pelagabacter ubique.,Schuller DJ, Reisch CR, Moran MA, Whitman WB, Lanzilotta WN Protein Sci. 2011 Dec 7. doi: 10.1002/pro.2015. PMID:22162093 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminomethyltransferase

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