【2h】

Structure of the secretion domain of HxuA from Haemophilus influenzae

机译:流感嗜血杆菌HxuA分泌域的结构

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摘要

Haemophilus influenzae HxuA is a cell-surface protein with haem–haemopexin binding activity which is key to haem acquisition from haemopexin and thus is one of the potential sources of haem for this microorganism. HxuA is secreted by its specific transporter HxuB. HxuA/HxuB belongs to the so-called two-partner secretion systems (TPSs) that are characterized by a conserved N-­terminal domain in the secreted protein which is essential for secretion. Here, the 1.5 Å resolution structure of the secretion domain of HxuA, HxuA301, is reported. The structure reveals that HxuA301 folds into a β-helix domain with two extra-helical motifs, a four-stranded β-sheet and an N-terminal cap. Comparisons with other structures of TpsA secretion domains are reported. They reveal that despite limited sequence identity, strong structural similarities are found between the β-helix motifs, consistent with the idea that the TPS domain plays a role not only in the interaction with the specific TpsB partners but also as the scaffold initiating progressive folding of the TpsA proteins at the bacterial surface.
机译:流感嗜血杆菌HxuA是一种具有血红素与血红素结合蛋白结合活性的细胞表面蛋白,是从血红素单抗中获取血红素的关键,因此是该微生物潜在的血红素来源之一。 HxuA由其特定的转运蛋白HxuB分泌。 HxuA / HxuB属于所谓的两伙伴分泌系统(TPSs),其特征在于分泌的蛋白质中保守的N-­末端结构域,这对于分泌至关重要。在此,报道了HxuA的分泌结构域HxuA301的1.5分辨率结构。该结构显示HxuA301折叠成具有两个螺旋外基序,四链β-折叠和N末端帽的β-螺旋结构域。报道了与TpsA分泌结构域的其他结构的比较。他们发现尽管序列同一性有限,但在β-螺旋基序之间却发现了很强的结构相似性,这与TPS结构域不仅在与特定TpsB伴侣的相互作用中起作用,而且在支架上开始逐步折叠的过程中都起作用有关。细菌表面的TpsA蛋白。

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