1hh1: Difference between revisions

Revision as of 08:10, 1 July 2008

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File:1hh1.png

Template:STRUCTURE 1hh1

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

Template:ABSTRACT PUBMED 11331763

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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OCA

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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===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11331763}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11331763}}
 ==About this Structure==
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 [[Category: Homologous recombination]]
 [[Category: Nuclease domain]]
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