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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution.
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Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution.

机译：交替构象中观察到催化丝氨酸的枯草芽孢杆菌脂肪酶在决定1.3一项决议。

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摘要

Bacillus subtilis extracellular lipase (BsL) has an exceptionally low molecular weight (19.4 kDa) for a member of the lipase family. A crystallographic study was performed on BsL in order to design and produce mutant BsL that will be more suitable for industrial uses based on analysis of the three-dimensional structure. Recently, the crystal structure of BsL has been determined at 1.5 A resolution [van Pouderoyen et al. (2001). J. Mol. Biol. 309, 215-226]. In the present study, a new crystal form of BsL which provides diffraction data to higher resolution was obtained and its structure was determined at 1.3 A using the MAD method. It was found that the active-site residue Ser77 has alternate side-chain conformations. The O(gamma) atom of the first conformer forms a hydrogen bond to the N(epsilon) atom of His155, a member of the catalytic triad. In contrast, the second conformer is constructed with a hydrogen bond to the side-chain atom of the adjacent His76. These two conformers presumably correspond to the active and inactive states, respectively. Similar alternate conformations in the catalytic serine residue have been observed in Fusarium solani cutinase determined at 1.0 A resolution and Penicillium purpurogenum acetylxylan esterase at 0.9 A resolution. In addition, a glycerol molecule, which was used as a cryoprotectant, is found to be located in the active site. On the basis of these results, a model for substrate binding in the reaction-intermediate state of BsL is proposed.
机译：枯草芽孢杆菌胞外脂肪酶(声波测井)异常低分子量(19.4 kDa)对脂肪酶家族的一员。晶体研究声波测井为了设计和产生突变声波测井更适合工业用途基于三维结构的分析。最近,声波测井的晶体结构确定在1.5 (van Pouderoyen等决议艾尔。(2001)。目前的研究中,一个新的水晶的声波测井提供更高分辨率的衍射数据是获得,其结构是决定在哪里1.3使用疯狂的方法。活性位点残Ser77备用侧链构象。第一个构象异构体形成的氢键His155 N(ε)原子,的一员催化三和弦。构象异构体是由氢键的侧链原子邻His76。两个矫形器可能对应分别活跃的和不活跃的状态。催化丝氨酸替代构象残留在腐皮镰刀菌被观察到cutinase 1.0决议和决定青霉菌purpurogenum acetylxylan酯酶0.9一项决议。分子,作为冷冻保护剂,位于活性部位。基于这些结果,衬底的典范绑定在声波测井的反应中间体状态提出了。

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