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首页> 外文期刊>Acta crystallographica. Section D, Structural biology >A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat
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A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat

机译：一个反复出现的包装InlB晶体的联系确定了功能的结合位点internalin域和重复

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摘要

InlB, a bacterial agonist of the human receptor tyrosine kinase MET, consists of an N‐terminal internalin domain, a central B repeat and three C‐terminal GW domains. In all previous structures of full‐length InlB or an InlB construct lacking the GW domains (InlB392), there was no interpretable electron density for the B repeat. Here, three InlB392 crystal structures in which the B repeat is resolved are described. These are the first structures to reveal the relative orientation of the internalin domain and the B repeat. A wild‐type structure and two structures of the T332E variant together contain five crystallographically independent molecules. Surprisingly, the threonine‐to‐glutamate substitution in the B repeat substantially improved the crystallization propensity and crystal quality of the T332E variant. The internalin domain and B repeat are quite rigid internally, but are flexibly linked to each other. The new structures show that inter‐domain flexibility is the most likely cause of the missing electron density for the B repeat in previous InlB structures. A potential binding groove between B‐repeat strand β2 and an adjacent loop forms an important crystal contact in all five crystallographically independent chains. This region may represent a hydrophobic `sticky patch' that supports protein–protein interactions. This assumption agrees with the previous finding that all known inactivating point mutations in the B repeat lie within strand β2. The groove formed by strand β2 and the adjacent loop may thus represent a functionally important protein–protein interaction site in the B repeat.
机译：InlB,细菌的人类受体激动剂酪氨酸激酶,由一个N终端internalin域,一个中央B和三个重复C检测终端GW域。全量长度InlB或InlB构造缺乏GW域(InlB392),没有可说明的电子密度的重复。在这里,三个InlB392晶体结构B重复解决。第一个结构,揭示了相对的取向的internalin域和B重复。包含5个一起的T332E变体结晶学独立的分子。令人惊讶的是,苏氨酸~谷氨酸在B替换重复提高了结晶倾向水晶T332E变体的质量。internalin域和B重复相当严格在内部,但灵活是相互连接的其他。灵活性是最有可能的原因失踪的B重复的电子密度以前InlB结构。B槽之间的重复链β2和一个相邻循环形成一个重要的晶体接触五个结晶学独立的连锁店。这个区域可能代表一个疏水的粘性支持蛋白质的补丁”交互。之前的发现,所有已知的灭活点突变在B链内重复的谎言β2。因此,相邻的循环可能代表一个功能重要的蛋白质交互网站B重复。

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