1hh1: Difference between revisions
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[[Image:1hh1.gif|left|200px]] | [[Image:1hh1.gif|left|200px]] | ||
'''THE STRUCTURE OF HJC, A HOLLIDAY JUNCTION RESOLVING ENZYME FROM SULFOLOBUS SOLFATARICUS''' | {{Structure | ||
|PDB= 1hh1 |SIZE=350|CAPTION= <scene name='initialview01'>1hh1</scene>, resolution 2.15Å | |||
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|LIGAND= | |||
|ACTIVITY= | |||
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'''THE STRUCTURE OF HJC, A HOLLIDAY JUNCTION RESOLVING ENZYME FROM SULFOLOBUS SOLFATARICUS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HH1 is a [ | 1HH1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HH1 OCA]. | ||
==Reference== | ==Reference== | ||
Structure of Hjc, a Holliday junction resolvase, from Sulfolobus solfataricus., Bond CS, Kvaratskhelia M, Richard D, White MF, Hunter WN, Proc Natl Acad Sci U S A. 2001 May 8;98(10):5509-14. Epub 2001 May 1. PMID:[http:// | Structure of Hjc, a Holliday junction resolvase, from Sulfolobus solfataricus., Bond CS, Kvaratskhelia M, Richard D, White MF, Hunter WN, Proc Natl Acad Sci U S A. 2001 May 8;98(10):5509-14. Epub 2001 May 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11331763 11331763] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfolobus solfataricus]] | [[Category: Sulfolobus solfataricus]] | ||
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[[Category: nuclease domain]] | [[Category: nuclease domain]] | ||
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Revision as of 12:37, 20 March 2008
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THE STRUCTURE OF HJC, A HOLLIDAY JUNCTION RESOLVING ENZYME FROM SULFOLOBUS SOLFATARICUS
OverviewOverview
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.
About this StructureAbout this Structure
1HH1 is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of Hjc, a Holliday junction resolvase, from Sulfolobus solfataricus., Bond CS, Kvaratskhelia M, Richard D, White MF, Hunter WN, Proc Natl Acad Sci U S A. 2001 May 8;98(10):5509-14. Epub 2001 May 1. PMID:11331763
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