1ob9

Holliday Junction Resolving Enzyme

spinqualitylabelsall models 1ob9, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ob9 is a 1 chain structure with sequence from Atcc 35091. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, FMT Related: 1ob8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HJE_SULSO] A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Acts only on 4-way DNA junctions in a sequence non-specific manner; introduces paired nicks in opposing strands 2 bases 3' of the point of strand exchange only on continuous strands of 4-way junction DNA. Cleaves both mobile and immobile junctions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Two archaeal Holliday junction resolving enzymes, Holliday junction cleavage (Hjc) and Holliday junction endonuclease (Hje), have been characterized. Both are members of a nuclease superfamily that includes the type II restriction enzymes, although their DNA cleaving activity is highly specific for four-way junction structure and not nucleic acid sequence. Despite 28% sequence identity, Hje and Hjc cleave junctions with distinct cutting patterns--they cut different strands of a four-way junction, at different distances from the junction centre. We report the high-resolution crystal structure of Hje from Sulfolobus solfataricus. The structure provides a basis to explain the differences in substrate specificity of Hje and Hjc, which result from changes in dimer organization, and suggests a viral origin for the Hje gene. Structural and biochemical data support the modelling of an Hje:DNA junction complex, highlighting a flexible loop that interacts intimately with the junction centre. A highly conserved serine residue on this loop is shown to be essential for the enzyme's activity, suggesting a novel variation of the nuclease active site. The loop may act as a conformational switch, ensuring that the active site is completed only on binding a four-way junction, thus explaining the exquisite specificity of these enzymes. Substrate recognition and catalysis by the Holliday junction resolving enzyme Hje.,Middleton CL, Parker JL, Richard DJ, White MF, Bond CS Nucleic Acids Res. 2004 Oct 12;32(18):5442-51. Print 2004. PMID:15479781 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Resolvase 3D structures

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