8Q1V

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

Summary for 8Q1V

• Entry DOI: 10.2210/pdb8q1v/pdb
• Descriptor: Putative lipoprotein, HEME C, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: cytochrome, redox, x183, cazy, electron transport
• Biological source: Teredinibacter turnerae
• Total number of polymer chains: 1
• Total formula weight: 10625.89

Authors

Rajagopal, B.S.,Hemsworth, G.R. (deposition date: 2023-08-01, release date: 2024-03-13, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.4 Å)