1hh1
From Proteopedia
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| - | [[Image:1hh1.gif|left|200px]] | + | [[Image:1hh1.gif|left|200px]] |
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| - | '''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 | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:36:58 2008'' |
Revision as of 09:37, 20 March 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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