Binbuga Bulent, Boroujerdi Arezue F B, Young John K
Department of Chemistry, Mississippi State University, Mississippi State, Mississippi 39762, USA.
Protein Sci. 2007 Aug;16(8):1783-7. doi: 10.1110/ps.072950407.
Proteins from halophiles have adapted to challenging environmental conditions and require salt for their structure and function. How halophilic proteins adapted to a hypersaline environment is still an intriguing question. It is important to mimic the physiological conditions of the archae extreme halophiles when characterizing their enzymes, including structural characterization. The NMR derived structure of Haloferax volcanii dihydrofolate reductase in 3.5 M NaCl is presented, and represents the first high salt structure calculated using NMR data. Structure calculations show that this protein has a solution structure which is similar to the previously determined crystal structure with a difference at the N terminus of beta3 and the type of beta-turn connection beta7 and beta8.
嗜盐菌的蛋白质已适应具有挑战性的环境条件，并且其结构和功能需要盐的存在。嗜盐蛋白质如何适应高盐环境仍是一个引人入胜的问题。在表征嗜盐古菌的酶（包括结构表征）时，模拟其生理条件非常重要。本文展示了嗜盐栖热袍菌二氢叶酸还原酶在3.5 M氯化钠中的核磁共振衍生结构，这是首个使用核磁共振数据计算得到的高盐结构。结构计算表明，该蛋白质的溶液结构与先前确定的晶体结构相似，但在β3的N端以及β7和β8之间的β-转角连接类型上存在差异。
