Arndt Joseph W, Gu Jenny, Jaroszewski Lukasz, Schwarzenbacher Robert, Hanson Michael A, Lebeda Frank J, Stevens Raymond C
Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA.
J Mol Biol. 2005 Mar 4;346(4):1083-93. doi: 10.1016/j.jmb.2004.12.039. Epub 2005 Jan 20.
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 A 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.
肉毒杆菌的血凝蛋白HA33与大型肉毒杆菌神经毒素分泌复合物相关，在毒素保护、内化以及可能的激活过程中起关键作用。我们报道了A型HA33（HA33/A）在1.5埃分辨率下的晶体结构，其包含独特的结构域组织和一个碳水化合物识别位点。此外，对其他毒素复合物成分（包括神经毒素BoNT/A、血凝蛋白HA17/A和无毒无血凝蛋白NTNHA/A）的序列比对表明，大多数毒素复合物由重复出现的β-三叶折叠组成。
