Structural dissection of two redox proteins from the shipworm symbiont Teredinibacter turnerae
Structural dissection of two redox proteins from the shipworm symbiont Teredinibacter turnerae
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DOI：
10.1107/s2052252524001386
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发表时间：
2024-03-01
期刊：
影响因子：
3.9
通讯作者：
Hemsworth，Glyn R.
中科院分区：
文献类型：
--
作者：
Rajagopal，Badri S.;Yates，Nick;Hemsworth，Glyn R.
溶解性多糖单加氧酶（LPMO）是一类在多糖降解中起主要作用的铜依赖性酶家族，其发现揭示了氧化还原酶在生物质的生物利用中的重要性。在真菌中，一系列氧化还原蛋白与LPMO一起作用，导致多糖氧化。在细菌中，关于氧化还原蛋白和LPMO之间的相互作用，或者两者之间的相互作用如何有助于多糖降解，我们知之甚少。因此，我们着手表征两个以前未研究的蛋白质的船蛆共生体Teredinibacter turnerae，最初确定的碳水化合物结合结构域的存在下附加到未表征的结构域可能的氧化还原功能。在这里，从这些蛋白质的几个域的X射线晶体结构一起提出的初步努力，以表征其功能。分析表明，靶蛋白不太可能作为LPMO电子供体发挥作用，这就提出了新的问题，即这些大型细胞外含多血红素的C型细胞色素可能在这些细菌中发挥潜在的氧化还原功能。
The discovery of lytic polysaccharide monooxygenases (LPMOs), a family of copper-dependent enzymes that play a major role in polysaccharide degradation, has revealed the importance of oxidoreductases in the biological utilization of biomass. In fungi, a range of redox proteins have been implicated as working in harness with LPMOs to bring about polysaccharide oxidation. In bacteria, less is known about the interplay between redox proteins and LPMOs, or how the interaction between the two contributes to polysaccharide degradation. We therefore set out to characterize two previously unstudied proteins from the shipworm symbiont Teredinibacter turnerae that were initially identified by the presence of carbohydrate binding domains appended to uncharacterized domains with probable redox functions. Here, X-ray crystal structures of several domains from these proteins are presented together with initial efforts to characterize their functions. The analysis suggests that the target proteins are unlikely to function as LPMO electron donors, raising new questions as to the potential redox functions that these large extracellular multi-haem-containing c-type cytochromes may perform in these bacteria.