8Q1V

TtX183A - A c-type cytochrome domain from the Teredinibacter turnerae protein TERTU_2913

8Q1V の概要

• エントリーDOI: 10.2210/pdb8q1v/pdb
• 分子名称: Putative lipoprotein, HEME C, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: cytochrome, redox, x183, cazy, electron transport
• 由来する生物種: Teredinibacter turnerae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10625.89

構造登録者

Rajagopal, B.S.,Hemsworth, G.R. (登録日: 2023-08-01, 公開日: 2024-03-13, 最終更新日: 2024-11-20)

主引用文献

Rajagopal, B.S.,Yates, N.,Smith, J.,Paradisi, A.,Tetard-Jones, C.,Willats, W.G.T.,Marcus, S.,Knox, J.P.,Firdaus-Raih, M.,Henrissat, B.,Davies, G.J.,Walton, P.H.,Parkin, A.,Hemsworth, G.R.
Structural dissection of two redox proteins from the shipworm symbiont Teredinibacter turnerae.
Iucrj, 11:260-274, 2024

PubMed Abstract: 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.

PubMed: 38446458
DOI: 10.1107/S2052252524001386

実験手法

X-RAY DIFFRACTION (1.4 Å)