7mch

Crystal structure of a single-chain E/F type bilin lyase-isomerase MpeQ in space group C2221

spinqualitylabelsall models 7mch, resolution 2.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7mch is a 2 chain structure with sequence from Synechococcus sp. A15-62. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.95Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function U3MW57_9SYNE Publication Abstract from PubMed Chromophore attachment of the light-harvesting apparatus represents one of the most important post-translational modifications in photosynthetic cyanobacteria. Extensive pigment diversity of cyanobacteria critically depends on bilin lyases that covalently attach chemically distinct chromophores to phycobiliproteins. However, how bilin lyases catalyze bilin ligation reactions and how some lyases acquire additional isomerase abilities remain elusive at the molecular level. Here, we report the crystal structure of a representative bilin lyase-isomerase MpeQ. This structure has revealed a "question-mark" protein architecture that unambiguously establishes the active site conserved among the E/F-type bilin lyases. Based on structural, mutational, and modeling data, we demonstrate that stereoselectivity of the active site plays a critical role in conferring the isomerase activity of MpeQ. We further advance a tyrosine-mediated reaction scheme unifying different types of bilin lyases. These results suggest that lyases and isomerase actions of bilin lyases arise from two coupled molecular events of distinct origin. Crystal structure and molecular mechanism of an E/F type bilin lyase-isomerase.,Kumarapperuma I, Joseph KL, Wang C, Biju LM, Tom IP, Weaver KD, Grebert T, Partensky F, Schluchter WM, Yang X Structure. 2022 Feb 2. pii: S0969-2126(22)00007-7. doi:, 10.1016/j.str.2022.01.007. PMID:35148828 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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