Department of Life Sciences, Imperial College London, London SW7 2AZ, UK.
Biochim Biophys Acta Proteins Proteom. 2017 Apr;1865(4):422-433. doi: 10.1016/j.bbapap.2017.01.006. Epub 2017 Jan 24.
The critical need for iron presents a challenge for pathogenic bacteria that must survive in an environment bereft of accessible iron due to a natural low bioavailability and their host's nutritional immunity. Appropriating haem, either direct from host haemoproteins or by secreting haem-scavenging haemophores, is one way pathogenic bacteria can overcome this challenge. After capturing their target, haem appropriation systems must remove haem from a high-affinity binding site (on the host haemoprotein or bacterial haemophore) and transfer it to a binding site of lower affinity on a bacterial receptor. Structural information is now available to show how, using a combination of induced structural changes and steric clashes, bacteria are able to extract haem from haemophores, haemopexin and haemoglobin. This review focuses on structural descriptions of these bacterial haem acquisition systems, summarising how they bind haem and their target haemoproteins with particularly emphasis on the mechanism of haem extraction.
对致病菌而言,铁是一种关键的必需营养物质,但由于其天然生物利用度低,且宿主存在营养免疫,导致其在缺乏可利用铁的环境中难以存活。致病菌可以通过直接从宿主血红素蛋白中获取血红素,或通过分泌血红素结合蛋白来摄取血红素,从而解决这一难题。在捕获其靶标后,血红素摄取系统必须将血红素从高亲和力结合位点(在宿主血红素蛋白或细菌血红素结合蛋白上)转移到细菌受体上亲和力较低的结合位点。目前已有结构信息可显示,致病菌如何利用诱导的结构变化和空间位阻,从血红素结合蛋白、血红素结合蛋白和血红蛋白中提取血红素。本综述重点介绍了这些细菌血红素摄取系统的结构描述,总结了它们与血红素及其靶血红素蛋白的结合方式,特别强调了血红素提取的机制。