7bnx | pdb_00007bnx

Archeal holliday junction resolvase from Thermus thermophilus phage 15-6

spinqualitylabelsall models 7bnx, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7bnx is a 2 chain structure with sequence from Unclassified bacterial viruses. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.551Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed This study describes the production, characterization and structure determination of a novel Holliday junction-resolving enzyme. The enzyme, termed Hjc_15-6, is encoded in the genome of phage Tth15-6, which infects Thermus thermophilus. Hjc_15-6 was heterologously produced in Escherichia coli and high yields of soluble and biologically active recombinant enzyme were obtained in both complex and defined media. Amino-acid sequence and structure comparison suggested that the enzyme belongs to a group of enzymes classified as archaeal Holliday junction-resolving enzymes, which are typically divalent metal ion-binding dimers that are able to cleave X-shaped dsDNA-Holliday junctions (Hjs). The crystal structure of Hjc_15-6 was determined to 2.5 A resolution using the selenomethionine single-wavelength anomalous dispersion method. To our knowledge, this is the first crystal structure of an Hj-resolving enzyme originating from a bacteriophage that can be classified as an archaeal type of Hj-resolving enzyme. As such, it represents a new fold for Hj-resolving enzymes from phages. Characterization of the structure of Hjc_15-6 suggests that it may form a dimer, or even a homodimer of dimers, and activity studies show endonuclease activity towards Hjs. Furthermore, based on sequence analysis it is proposed that Hjc_15-6 has a three-part catalytic motif corresponding to E-SD-EVK, and this motif may be common among other Hj-resolving enzymes originating from thermophilic bacteriophages. Crystal structure and initial characterization of a novel archaeal-like Holliday junction-resolving enzyme from Thermus thermophilus phage Tth15-6.,Ahlqvist J, Linares-Pasten JA, Hakansson M, Jasilionis A, Kwiatkowska-Semrau K, Friethjonsson OH, Kaczorowska AK, Dabrowski S, AEvarsson A, Hreggviethsson GO, Al-Karadaghi S, Kaczorowski T, Nordberg Karlsson E Acta Crystallogr D Struct Biol. 2022 Feb 1;78(Pt 2):212-227. doi:, 10.1107/S2059798321012298. Epub 2022 Jan 24. PMID:35102887 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Resolvase 3D structures

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