The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring β-trefoil fold in the progenitor toxin complex
The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring β-trefoil fold in the progenitor toxin complex
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DOI：
10.1016/j.jmb.2004.12.039
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发表时间：
2005-03-04
影响因子：
5.6
通讯作者：
Stevens, RC
中科院分区：
文献类型：
--
作者：
Arndt, JW;Gu, J;Stevens, RC
肉毒梭菌的血凝蛋白HA33与大的肉毒神经毒素分泌复合体有关，在毒素保护、内化和可能的激活中起关键作用。我们报道了A型HA33(HA33/A)在1.5埃分辨率下的晶体结构，其中包含一个独特的结构域组织和一个碳水化合物识别位点。此外，对其他毒素复合体成分，包括神经毒素BONT/A、血凝蛋白HA17/A和无毒非血凝蛋白NTNHA/A的序列比对表明，大多数毒素复合体由重复出现的β-三叶折叠组成。(C)2004爱思唯尔有限公司。保留所有权利。
The hemagglutinating protein HA33 from Clostridium botulinum is associated with the large botulinum neurotoxin secreted complexes and is critical in toxin protection, internalization, and possibly activation. We report the crystal structure of serotype A HA33 (HA33/A) at 1.5 Angstrom resolution that contains a unique domain organization and a carbohydrate recognition site. In addition, sequence alignments of the other toxin complex components, including the neurotoxin BoNT/A, hemagglutinating protein HA17/A, and non-toxic non-hemagglutinating protein NTNHA/A, suggests that most of the toxin complex consists of a reoccurring beta-trefoil fold. (C) 2004 Elsevier Ltd. All rights reserved.