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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Three-dimensional structure of homodimeric cholesterol esterase-ligand complex at 1.4 A resolution.
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Three-dimensional structure of homodimeric cholesterol esterase-ligand complex at 1.4 A resolution.

机译：三维结构的homodimeric胆固醇在1.4 esterase-ligand复杂决议。

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摘要

The three-dimensional structure of a Candida cylindracea cholesterol esterase (ChE) homodimer (534 x 2 amino acids) in complex with a ligand of proposed formula C(23)H(48)O(2) has been determined at 1.4 A resolution in space group P1 using synchrotron low-temperature data. The structure refined to R = 0.136 and R(free) = 0.169 and has revealed new stereochemical details in addition to those detected for the apo- and holo-forms at 1.9 and 2.0 A resolution, respectively [Ghosh et al. (1995), Structure, 3, 279-288]. The cholesterol esterase structure is a dimer with four spatially separated interfacial contact areas and two symmetry-related pairs of openings to an internal intradimer cavity. Hydrophobic active-site gorges in each subunit face each other across a central interfacial cavity. The ChE subunits have carbohydrate chains attached to their Asn314 and Asn351 residues, with two ordered N-acetyl-D-glucosoamine moieties visible at each site. The side chains of 14 residues have two alternative conformations with occupancy values of 0.5 +/- 0.2. For each subunit the electron density in the enzyme active-site gorge is well modeled by a C(23)-chain fatty acid.
机译：念珠菌的三维结构茶树菇胆固醇酯酶(切)为(534 x 2氨基酸)在复杂的配体提出公式C (23) H (48) O (2)在空间群P1 1.4决议决定使用同步加速器低温数据。结构优化和R(免费)= R = 0.1360.169和揭示了新的立体化学的细节除了这些发现“分离”和holo-forms分辨率1.9和2.0,分别[Ghosh et al。(1995),结构,3,279 - 288年)。二聚体与四个空间界面分开接触区域和两个symmetry-related双内部intradimer腔开口。每个亚基疏水活性部位峡谷面对面跨中心界面腔。附加到Asn314 Asn351残留物,有两个命令N-acetyl-D-glucosoamine根在每个站点上可见。残留有两种构象入住率的值0.5 + / - 0.2。酶活性部位的电子密度峡谷是由一个C(23)链脂肪酸。

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