流感嗜血杆菌血红素结合蛋白结构的建模表明了一种血红素相互作用模式。
Modeling of the structure of the Haemophilus influenzae heme-binding protein suggests a mode of heme interaction.
作者信息
Dunten P, Mowbray S L
机构信息
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala, Sweden.
出版信息
Protein Sci. 1995 Nov;4(11):2335-40. doi: 10.1002/pro.5560041111.
Abstract
The structure and function of the periplasmic heme-binding protein HbpA of Haemophilus influenzae were investigated. This protein is involved in the import of heme into the bacteria through the inner membrane, and thus is a key element of the organism's ability to survive in blood. A high degree of sequence similarity between HbpA and the dipeptide-binding protein of Escherichia coli is suggested to be the result of a functional relationship. An HbpA model built using the dipeptide-binding protein suggests a mode of heme binding that is distinct from those known in proteins of the human host. These results provide a starting point for rational drug design.
摘要
对流感嗜血杆菌周质血红素结合蛋白HbpA的结构和功能进行了研究。该蛋白通过内膜参与血红素向细菌内的转运，因此是该生物体在血液中生存能力的关键要素。HbpA与大肠杆菌二肽结合蛋白之间高度的序列相似性被认为是功能关系的结果。利用二肽结合蛋白构建的HbpA模型表明了一种与人类宿主蛋白中已知的血红素结合模式不同的模式。这些结果为合理的药物设计提供了一个起点。
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