6y01

The structure of the molybdenum cofactor binding protein from the phototrophic bacterium Rippkaea orientalis

spinqualitylabelsall models 6y01, resolution 1.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6y01 is a 4 chain structure with sequence from Rippkaea orientalis PCC 8801. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.23Å Ligands: CL, IMD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7K4Z0_RIPO1 Publication Abstract from PubMed The molybdenum cofactor (Moco) is the prosthetic group of all molybdenum-dependent enzymes except for nitrogenase. The multistep biosynthesis pathway of Moco and its function in molybdenum-dependent enzymes are already well understood. The mechanisms of Moco transfer, storage and insertion, on the other hand, are not. In the cell, Moco is usually not found in its free form and remains bound to proteins because of its sensitivity to oxidation. The green alga Chlamydomonas reinhardtii harbors a Moco carrier protein (MCP) that binds and protects Moco but is devoid of enzymatic function. It has been speculated that this MCP acts as a means of Moco storage and transport. Here, the search for potential MCPs has been extended to the prokaryotes, and many MCPs were found in cyanobacteria. A putative MCP from Rippkaea orientalis (RoMCP) was selected for recombinant production, crystallization and structure determination. RoMCP has a Rossmann-fold topology that is characteristic of nucleotide-binding proteins and a homotetrameric quaternary structure similar to that of the MCP from C. reinhardtii. In each protomer, a positively charged crevice was identified that accommodates up to three chloride ions, hinting at a potential Moco-binding site. Computational docking experiments supported this notion and gave an impression of the RoMCP-Moco complex. The structure of the Moco carrier protein from Rippkaea orientalis.,Krausze J, Hercher TW, Archna A, Kruse T Acta Crystallogr F Struct Biol Commun. 2020 Sep 1;76(Pt 9):453-463. doi:, 10.1107/S2053230X20011073. Epub 2020 Aug 28. PMID:32880594 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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