1hh1
From Proteopedia
(New page: 200px<br /><applet load="1hh1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hh1, resolution 2.15Å" /> '''THE STRUCTURE OF HJC...) |
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| - | [[Image:1hh1.gif|left|200px]]<br /><applet load="1hh1" size=" | + | [[Image:1hh1.gif|left|200px]]<br /><applet load="1hh1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hh1, resolution 2.15Å" /> | caption="1hh1, resolution 2.15Å" /> | ||
'''THE STRUCTURE OF HJC, A HOLLIDAY JUNCTION RESOLVING ENZYME FROM SULFOLOBUS SOLFATARICUS'''<br /> | '''THE STRUCTURE OF HJC, A HOLLIDAY JUNCTION RESOLVING ENZYME FROM SULFOLOBUS SOLFATARICUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 2.15-A structure of Hjc, a Holliday junction-resolving enzyme from the | + | 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 Structure== | ==About this Structure== | ||
| - | 1HH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http:// | + | 1HH1 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfolobus solfataricus]] | [[Category: Sulfolobus solfataricus]] | ||
| - | [[Category: Bond, C | + | [[Category: Bond, C S.]] |
| - | [[Category: Hunter, W | + | [[Category: Hunter, W N.]] |
[[Category: Kvaratskhelia, M.]] | [[Category: Kvaratskhelia, M.]] | ||
[[Category: Richard, D.]] | [[Category: Richard, D.]] | ||
| - | [[Category: White, M | + | [[Category: White, M F.]] |
[[Category: archaea]] | [[Category: archaea]] | ||
[[Category: holliday junction resolvase]] | [[Category: holliday junction resolvase]] | ||
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[[Category: nuclease domain]] | [[Category: nuclease domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:10 2008'' |
Revision as of 11:01, 21 February 2008
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THE STRUCTURE OF HJC, A HOLLIDAY JUNCTION RESOLVING ENZYME FROM SULFOLOBUS SOLFATARICUS
Overview
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 Structure
1HH1 is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
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:11331763
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