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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Extraction of functional motion in trypsin crystal structures
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Extraction of functional motion in trypsin crystal structures

机译：提取胰蛋白酶水晶的功能运动结构

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摘要

The analysis of anisotropic atomic displacement parameters for the direct extraction of functionally relevant motion from X-ray crystal structures of Fusarium oxysporum trypsin is presented. Several atomic resolution structures complexed with inhibitors or substrates and determined at different pH values and temperatures were investigated. The analysis revealed a breathing-like molecular motion conserved across trypsin structures from two organisms and three different crystal forms. Directional motion was observed suggesting a change of the width of the substrate-binding cleft and a change in the length of the specificity pocket. The differences in direction of motion across the structures are dependent on the mode of substrate or inhibitor binding and the chemical environment around the active-site residues. Together with the occurrence of multiple-residue conformers, they reflect spatial rearrangement throughout the deacylation pathway.
机译：各向异性原子位移分析直接提取的参数从x射线晶体功能相关的运动结构的尖孢镰刀菌胰蛋白酶提出了。包裹着抑制剂或基质在不同的pH值和决定温度了。揭示了breathing-like分子运动从两个守恒在胰蛋白酶结构生物和三个不同的晶体形式。定向运动是观察到的暗示substrate-binding的宽度的变化裂和改变的长度特异性的口袋里。的整个结构都依赖于运动绑定和底物或抑制剂的模式活性位点周围的化学环境残留。multiple-residue矫形器,它们反映了空间整个脱酰作用通路的重排。

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