6l9c | pdb_00006l9c

Neutron structure of copper amine oxidase from Arthrobacter glibiformis at pD 7.4

spinqualitylabelsall models 6l9c, resolution 1.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6l9c is a 1 chain structure with sequence from "achromobacter_globiformis"_(conn_1928)_bergey_et_al._1930 "achromobacter globiformis" (conn 1928) bergey et al. 1930. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CU, NA NonStd Res: ASA, E9C, TPQ Activity: Primary-amine oxidase, with EC number 1.4.3.21 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Recent advances in neutron crystallographic studies have provided structural bases for quantum behaviors of protons observed in enzymatic reactions. Thus, we resolved the neutron crystal structure of a bacterial copper (Cu) amine oxidase (CAO), which contains a prosthetic Cu ion and a protein-derived redox cofactor, topa quinone (TPQ). We solved hitherto unknown structures of the active site, including a keto/enolate equilibrium of the cofactor with a nonplanar quinone ring, unusual proton sharing between the cofactor and the catalytic base, and metal-induced deprotonation of a histidine residue that coordinates to the Cu. Our findings show a refined active-site structure that gives detailed information on the protonation state of dissociable groups, such as the quinone cofactor, which are critical for catalytic reactions. Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing.,Murakawa T, Kurihara K, Shoji M, Shibazaki C, Sunami T, Tamada T, Yano N, Yamada T, Kusaka K, Suzuki M, Shigeta Y, Kuroki R, Hayashi H, Yano T, Tanizawa K, Adachi M, Okajima T Proc Natl Acad Sci U S A. 2020 May 5. pii: 1922538117. doi:, 10.1073/pnas.1922538117. PMID:32371483 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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