The 3 Å resolution crystal structure of the Pseudomonas aeruginosa virulence factor CbpD both supports and challenges the current model of how lytic polysaccharide monooxygenases bind chitin and raises interesting possibilities about how type 2 secretion-system substrates may interact with the secretion machinery. This structure also demonstrates the utility of new, AI-powered, protein structure-prediction algorithms in making challenging structural targets tractable.
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机译:铜绿假单胞菌毒力因子 CbpD 的 3 Å 分辨率晶体结构既支持又挑战了当前裂解多糖单加氧酶如何结合几丁质的模型,并提出了关于 2 型分泌系统底物如何与分泌机制相互作用的有趣可能性。这种结构还证明了新的、人工智能驱动的蛋白质结构预测算法在使具有挑战性的结构靶点易于处理方面的效用。
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