The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix
The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix
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DOI：
10.1016/s0022-2836(03)00857-x
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发表时间：
2003-08-29
影响因子：
5.6
通讯作者：
Littlechild, JA
中科院分区：
文献类型：
--
作者：
Guy, JE;Isupov, MN;Littlechild, JA
利用多重反常色散技术，利用天然锌离子的信号，对嗜热古菌Aeropyrum pernix重组中链乙醇脱氢酶（ADH）的结构进行了解析。该酶是具有222点群对称性的四聚体。ADH单体由催化和辅因子结合结构域形成，其整体折叠类似于先前解决的ADH结构。1.62埃分辨率A. pernix ADH结构是holo形式，其中辅因子NADH结合到两个结构域之间的裂缝中。在活性位点中发现的电子密度被解释为辛酸，辛酸已被证明是酶的抑制剂。该抑制剂的位置与其羰基氧原子形成催化锌离子的第四配体。每个单体的结构锌离子仅以部分占据存在，并且在其不存在时形成二硫键。提高了A. pernix ADH被认为主要由亚基界面上增加的离子和疏水相互作用引起。(C)2003 Elsevier Ltd.保留所有权利。
The structure of the recombinant medium chain alcohol dehydrogenase (ADH) from the hyperthermophilic archaeon Aeropyrum pernix has been solved by the multiple anomalous dispersion technique using the signal from the naturally occurring zinc ions. The enzyme is a tetramer with 222 point group symmetry. The ADH monomer is formed from a catalytic and a cofactor-binding domain, with the overall fold similar to previously solved ADH structures. The 1.62 Angstrom resolution A. pernix ADH structure is that of the holo form, with the cofactor NADH bound into the cleft between the two domains. The electron density found in the active site has been interpreted to be octanoic acid, which has been shown to be an inhibitor of the enzyme. This inhibitor is positioned with its carbonyl oxygen atom forming the fourth ligand of the catalytic zinc ion. The structural zinc ion of each monomer is present at only partial occupancy and in its absence a disulfide bond is formed. The enhanced thermal stability of the A. pernix ADH is thought to arise primarily from increased ionic and hydrophobic interactions on the subunit interfaces. (C) 2003 Elsevier Ltd. All rights reserved.