1hh1: Difference between revisions

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[[Image:1hh1.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_1hh1|  PDB=1hh1  |  SCENE=  }}  
{{STRUCTURE_1hh1|  PDB=1hh1  |  SCENE=  }}  


'''THE STRUCTURE OF HJC, A HOLLIDAY JUNCTION RESOLVING ENZYME FROM SULFOLOBUS SOLFATARICUS'''
===THE STRUCTURE OF HJC, A HOLLIDAY JUNCTION RESOLVING ENZYME FROM SULFOLOBUS SOLFATARICUS===




==Overview==
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The 2.15-A structure of Hjc, a Holliday junction-resolving enzyme from the archaeon Sulfolobus solfataricus, reveals extensive structural homology with a superfamily of nucleases that includes type II restriction enzymes. Hjc is a dimer with a large DNA-binding surface consisting of numerous basic residues surrounding the metal-binding residues of the active sites. Residues critical for catalysis, identified on the basis of sequence comparisons and site-directed mutagenesis studies, are clustered to produce two active sites in the dimer, about 29 A apart, consistent with the requirement for the introduction of paired nicks in opposing strands of the four-way DNA junction substrate. Hjc displays similarity to the restriction endonucleases in the way its specific DNA-cutting pattern is determined but uses a different arrangement of nuclease subunits. Further structural similarity to a broad group of metal/phosphate-binding proteins, including conservation of active-site location, is observed. A high degree of conservation of surface electrostatic character is observed between Hjc and T4-phage endonuclease VII despite a complete lack of structural homology. A model of the Hjc-Holliday junction complex is proposed, based on the available functional and structural data.
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==About this Structure==
==About this Structure==
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[[Category: Homologous recombination]]
[[Category: Homologous recombination]]
[[Category: Nuclease domain]]
[[Category: Nuclease domain]]
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