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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of an acidic phospholipase A(2) from Indian saw-scaled viper (Echis carinatus) at 2.6 A resolution reveals a novel intermolecular interaction.
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Structure of an acidic phospholipase A(2) from Indian saw-scaled viper (Echis carinatus) at 2.6 A resolution reveals a novel intermolecular interaction.

机译：结构的酸性磷脂酶(2)印度锯鳞蝮蛇(Echis鳍)为2.6一项决议,揭示了一种新颖的分子间交互。

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摘要

The crystal structure of an acidic phospholipase A(2) from the venom of Echis carinatus (saw-scaled viper; scPLA(2)) has been determined at 2.6 A resolution and refined to a crystallographic R factor of 0.192. Although the overall structure of scPLA(2) is essentially similar to those of other group II acidic PLA(2)s from different species, it shows unique features in several parts. Particularly noteworthy is the C-terminal part, which folds differently to those of other group II PLA(2)s. This part is considered to be responsible for inhibition of the platelet-aggregation activity. The calcium-binding loop is tightly organized with sevenfold coordination. Another striking feature of scPLA(2) is the involvement of Asn79 O(delta1) of a symmetry-related molecule in a coordination linkage with Ca(2+) of the calcium-binding loop. This is the first observation of an internal metal ion participating in an intermolecular interaction. The beta-wing of a molecule is deeply inserted into the hydrophobic channel ofanother molecule and forms several intermolecular interactions. This results in the formation of an infinite chain of molecules. These chains are stacked in an antiparallel arrangement in the crystals.
机译：酸性磷脂酶的晶体结构(2) Echis毒液的鳍(锯鳞蝮蛇;2.6决议和精制晶体R因子为0.192。总体结构的scPLA(2)本质上是类似于另一组II酸性解放军(2)从不同的物种,它显示了独特的功能在几个部分。c端部分折叠过程不同另一组二世解放军(2)。被认为是负责抑制血小板聚集活动。钙结合循环组织严密七倍的协调。scPLA(2)的参与Asn79 O (delta1)symmetry-related分子的协调连杆与钙结合的Ca(2 +)循环。这是第一次观察到内部金属离子参与分子间交互。深深插入到疏水通道几个ofanother分子和形式分子间相互作用。无限的分子链的形成。这些链堆积在一个反平行的安排的晶体。

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