Abstract

The apo form of the double mutant of Wolinella succinogenes L-asparaginase (WAS) with V23Q and K24T substitutions in the flexible N-terminal loop (WASm), which exhibits an order of magnitude lower glutaminase activity compared to the wild-type enzyme, was crystallized in two modifications (sp. grs. P22₁2₁ and P2₁). The three-dimensional structure in two modifications was determined at 1.5 and 1.7 Å resolution, respectively. The three-dimensional structures and the molecular packing modes of the enzyme in two crystal modifications (monoclinic, sp. gr. P2₁, and orthorhombic, sp. gr. P22₁2₁) are compared. Intermolecular contacts and solvent channels in both crystal lattices are described. The orthorhombic crystals have a closer packing compared to the monoclinic crystals and lower water content (36.95 and 44.53%, respectively). However, the active sites in both structures are solvent accessible.

中文翻译：

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产自Wolinella succinigenes的L-天冬酰胺酶突变体的两种晶体修饰的分子堆积

摘要

在柔性N末端环（WASm）中具有V23Q和K24T取代的沃林氏菌琥珀酸L-天冬酰胺酶（WAS）双重突变体的载脂蛋白形式是谷氨酰胺酶活性比野生型酶低一个数量级。结晶在两个修饰（属遗传资源。P 22 ₁ 2 ₁和P 2 ₁）。在两个修改中的三维结构分别以1.5和1.7Å的分辨率确定。的三维结构和酶的两种晶体修饰（分子堆积模式单斜，比重= P 2 ₁，和斜方晶系，比重= P 22 ₁2 ₁）进行比较。描述了两个晶格中的分子间接触和溶剂通道。与单斜晶体相比，斜方晶体的堆积更紧密，含水量较低（分别为36.95％和44.53％）。但是，两个结构中的活性位点都是溶剂可及的。