7xrn | pdb_00007xrn

Ethanolamine ammonia-lyase complexed with AdoMeCbl in the presence of substrate

spinqualitylabelsall models 7xrn, resolution 2.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7xrn is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.07Å Ligands: B12, FWK, GOL, NH4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The X-ray structures of coenzyme B(12) (AdoCbl)-dependent eliminating isomerases complexed with adenosylmethylcobalamin (AdoMeCbl) have been determined. As judged from geometries, the Co-C bond in diol dehydratase (DD) is not activated even in the presence of substrate. In ethanolamine ammonia-lyase (EAL), the bond is elongated in the absence of substrate; in the presence of substrate, the complex likely exists in both pre- and post-homolysis states. The impacts of incorporating an extra CH(2) group are different in the two enzymes: the DD active site is flexible, and AdoMeCbl binding causes large conformational changes that make DD unable to adopt the catalytic state, whereas the EAL active site is rigid, and AdoMeCbl binding does not induce significant conformational changes. Such flexibility and rigidity of the active sites might reflect the tightness of adenine binding. The structures provide good insights into the basis of the very low activity of AdoMeCbl in these enzymes. Structural Insights into the Very Low Activity of the Homocoenzyme B(12) Adenosylmethylcobalamin in Coenzyme B(12) -Dependent Diol Dehydratase and Ethanolamine Ammonia-Lyase.,Shibata N, Higuchi Y, Krautler B, Toraya T Chemistry. 2022 Nov 21;28(65):e202202196. doi: 10.1002/chem.202202196. Epub 2022 , Sep 19. PMID:35974426 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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