4j49

PylD holoenzyme soaked with L-lysine-Ne-D-ornithine

spinqualitylabelsall models 4j49, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4j49 is a 2 chain structure with sequence from Methanosarcina barkeri str. Fusaro. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: 1J1, MG, NA, NAD, NAI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PYLD_METBF Catalyzes the ultimate step of the pyrrolysine biosynthesis pathway by converting the isopeptide (3R)-3-methyl-D-ornithyl-N(6)-L-lysine to the 22nd proteinogenic amino acid (PubMed:24916332). Is able to use surrogate substrates such as (3R)-D-ornithyl-N(6)-L-lysine in vitro (PubMed:23720358, PubMed:24916332). Publication Abstract from PubMed The final step in the biosynthesis of the 22nd genetically encoded amino acid, pyrrolysine, is catalyzed by PylD, a structurally and mechanistically unique dehydrogenase. This catalyzed reaction includes an induced-fit mechanism achieved by major structural rearrangements of the N-terminal helix upon substrate binding. Different steps of the reaction trajectory are visualized by complex structures of PylD with substrate and product. Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD).,Quitterer F, Beck P, Bacher A, Groll M Angew Chem Int Ed Engl. 2013 May 29. doi: 10.1002/anie.201301164. PMID:23720358 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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