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PDBsum entry 6l9c
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Oxidoreductase
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PDB id
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6l9c
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References listed in PDB file
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Key reference
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Title
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Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing.
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Authors
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T.Murakawa,
K.Kurihara,
M.Shoji,
C.Shibazaki,
T.Sunami,
T.Tamada,
N.Yano,
T.Yamada,
K.Kusaka,
M.Suzuki,
Y.Shigeta,
R.Kuroki,
H.Hayashi,
T.Yano,
K.Tanizawa,
M.Adachi,
T.Okajima.
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Ref.
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Proc Natl Acad Sci U S A, 2020,
117,
10818-10824.
[DOI no: ]
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PubMed id
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Abstract
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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.
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