1hh1: Difference between revisions

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[[Image:1hh1.gif|left|200px]]
[[Image:1hh1.gif|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hh1 OCA], [http://www.ebi.ac.uk/pdbsum/1hh1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hh1 RCSB]</span>
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'''THE STRUCTURE OF HJC, A HOLLIDAY JUNCTION RESOLVING ENZYME FROM SULFOLOBUS SOLFATARICUS'''
'''THE STRUCTURE OF HJC, A HOLLIDAY JUNCTION RESOLVING ENZYME FROM SULFOLOBUS SOLFATARICUS'''
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[[Category: Richard, D.]]
[[Category: Richard, D.]]
[[Category: White, M F.]]
[[Category: White, M F.]]
[[Category: archaea]]
[[Category: Archaea]]
[[Category: holliday junction resolvase]]
[[Category: Holliday junction resolvase]]
[[Category: homologous recombination]]
[[Category: Homologous recombination]]
[[Category: nuclease domain]]
[[Category: Nuclease domain]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:04:47 2008''

Revision as of 15:50, 2 May 2008

File:1hh1.gif

Template:STRUCTURE 1hh1

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 Page seeded by OCA on Fri May 2 18:50:17 2008

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