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首页> 外文期刊>Crystallography reports >Three-dimensional structure of laccase from Coriolus zonatus at 2.6 angstrom resolution
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Three-dimensional structure of laccase from Coriolus zonatus at 2.6 angstrom resolution

机译：2.6埃分辨率下的Coriolus zonatus漆酶的三维结构

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摘要

Laccase (oxygen oxidoreductase, EC 1.14.18.1) belongs to the copper-containing oxidases. This enzyme catalyzes reduction of molecular oxygen by different organic and inorganic compounds to water without the formation of hydrogen peroxide. The three-dimensional structure of native laccase from Coriolus zonatus was solved and refined at 2.6 angstrom resolution (R (factor) = 21.23%, R (free) = 23.82%, rms deviations for the bond lengths and bond angles are 0.008 angstrom and 1.19 degrees, respectively). The primary structure of the polypeptide chain and the architecture of the active site were refined. The carbohydrate component of the enzyme was identified. The access and exit water channels providing the access of molecular oxygen to the active site and release of water, which is the reduction product of molecular oxygen, from the protein molecule were found in the structure.
机译：漆酶（氧氧化还原酶，EC 1.14.18.1）属于含铜氧化酶。该酶催化分子氧被不同的有机和无机化合物还原为水，而不会形成过氧化氢。以2.6埃的分辨率（R（因子）= 21.23％，R（自由）= 23.82％）解析和精制了科氏菌天然漆酶的三维结构，结合长度和结合角的均方根偏差为0.008埃和1.19。度）。完善了多肽链的一级结构和活性位点的结构。鉴定了酶的碳水化合物成分。在结构中发现了进入和排出水通道，该通道提供了分子氧到达活性位点的通道，并释放了水，该水是分子氧的还原产物，从蛋白质分子中释放出来。

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