3fpj | pdb_00003fpj

Crystal Structure of E81Q mutant of MtNAS in complex with S-ADENOSYLMETHIONINE

spinqualitylabelsall models 3fpj, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fpj is a 2 chain structure with sequence from Metth. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: B3P, BR, SAM Related: 3fpe, 3fpf, 3fpg, 3fph Gene: MTH675 (METTH) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Nicotianamine (NA), a small molecule ubiquitous in plants, is an important divalent metal chelator and the main precursor of phytosiderophores. Nicotianamine synthase (NAS) is the enzyme catalyzing NA synthesis by the condensation of three aminopropyl moieties of S-adenosylmethionine (SAM) and the cyclization of one of them to form an azetidine ring. Here we report five crystal structures of an archaeal NAS from Methanothermobacter thermautotrophicus, either free or in complex with its product(s) and substrate(s). These structures reveal a two-domains fold arrangement of MtNAS, a small molecule related to NA (named here thermoNicotianamine or tNA), and an original mechanism of synthesis in a buried reaction chamber. This reaction chamber is open to the solvent through a small inlet, and a single active site allows the selective entrance of only one substrate at a time that is then processed and translocated stepwise. Crystallographic snapshots of iterative substrate translocations during nicotianamine synthesis in Archaea.,Dreyfus C, Lemaire D, Mari S, Pignol D, Arnoux P Proc Natl Acad Sci U S A. 2009 Sep 22;106(38):16180-4. Epub 2009 Sep 2. PMID:19805277 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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