1ob8: Difference between revisions

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[[Image:1ob8.jpg|left|200px]]
{{Seed}}
[[Image:1ob8.png|left|200px]]


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{{STRUCTURE_1ob8|  PDB=1ob8  |  SCENE=  }}  
{{STRUCTURE_1ob8|  PDB=1ob8  |  SCENE=  }}  


'''HOLLIDAY JUNCTION RESOLVING ENZYME'''
===HOLLIDAY JUNCTION RESOLVING ENZYME===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15479781}}


==About this Structure==
==About this Structure==
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[[Category: Nuclease]]
[[Category: Nuclease]]
[[Category: Thermophile]]
[[Category: Thermophile]]
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