Structure of Escherichia coli AdhP (ethanol-inducible dehydrogenase) with bound NAD
Structure of Escherichia coli AdhP (ethanol-inducible dehydrogenase) with bound NAD
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DOI：
10.1107/s1744309113015170
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发表时间：
2013-07-01
影响因子：
0.9
通讯作者：
Sims, Paul A.
中科院分区：
文献类型：
--
作者：
Thomas, Leonard M.;Harper, Angelica R.;Sims, Paul A.
AdhP是一种重组表达的来自大肠杆菌K-12（亚株MG 1655）的醇脱氢酶，其晶体结构被确定为2.01埃分辨率。使用分子置换解决的结构还包括结构和催化锌离子以及辅因子烟酰胺腺嘌呤二核苷酸（NAD）。晶体属P2（1）空间群，晶胞参数a = 68.18，B = 118.92，c = 97.87埃，β = 106.41度。最终的R因子和R-free分别为0.138和0.184。AdhP的活性位点的结构表明了一些可能参与质子中继的残基，并且AdhP的整体结构，包括与结构和活性位点锌离子的配位，与其他四聚醇脱氢酶的结构相似。
The crystal structure of AdhP, a recombinantly expressed alcohol dehydrogenase from Escherichia coli K-12 (substrain MG1655), was determined to 2.01 angstrom resolution. The structure, which was solved using molecular replacement, also included the structural and catalytic zinc ions and the cofactor nicotinamide adenine dinucleotide (NAD). The crystals belonged to space group P2(1), with unit-cell parameters a = 68.18, b = 118.92, c = 97.87 angstrom, beta = 106.41 degrees. The final R factor and R-free were 0.138 and 0.184, respectively. The structure of the active site of AdhP suggested a number of residues that may participate in a proton relay, and the overall structure of AdhP, including the coordination to structural and active-site zinc ions, is similar to those of other tetrameric alcohol dehydrogenase enzymes.