1hh1

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(Difference between revisions)

Revision as of 23:53, 10 September 2015

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

Structural highlights

1hh1 is a 1 chain structure with sequence from Atcc 35091. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[HJC_SULSO] A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination; may have some degree of sequence preference in a mobile junction. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products. Can cleave all 4 strands 3 bases 3' of the junction center. Cleaves both mobile and immobile junctions. Modifies the structure of the 4-way DNA junction, a model Holliday junction structure. The protein forms multiple complexes with 4-way DNA, suggesting more than 1 homodimer can bind to each junction.^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Charlebois RL, Singh RK, Chan-Weiher CC, Allard G, Chow C, Confalonieri F, Curtis B, Duguet M, Erauso G, Faguy D, Gaasterland T, Garrett RA, Gordon P, Jeffries AC, Kozera C, Kushwaha N, Lafleur E, Medina N, Peng X, Penny SL, She Q, St Jean A, van der Oost J, Young F, Zivanovic Y, Doolittle WF, Ragan MA, Sensen CW. Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2. Genome. 2000 Feb;43(1):116-36. PMID:10701121
↑ Kvaratskhelia M, White MF. Two Holliday junction resolving enzymes in Sulfolobus solfataricus. J Mol Biol. 2000 Apr 7;297(4):923-32. PMID:10736227 doi:http://dx.doi.org/10.1006/jmbi.2000.3624
↑ Kvaratskhelia M, Wardleworth BN, Norman DG, White MF. A conserved nuclease domain in the archaeal Holliday junction resolving enzyme Hjc. J Biol Chem. 2000 Aug 18;275(33):25540-6. PMID:10940317 doi:http://dx.doi.org/10.1074/jbc.M003420200
↑ Kvaratskhelia M, Wardleworth BN, Bond CS, Fogg JM, Lilley DM, White MF. Holliday junction resolution is modulated by archaeal chromatin components in vitro. J Biol Chem. 2002 Jan 25;277(4):2992-6. Epub 2001 Nov 14. PMID:11709558 doi:http://dx.doi.org/10.1074/jbc.M109496200
↑ Dorazi R, Parker JL, White MF. PCNA activates the Holliday junction endonuclease Hjc. J Mol Biol. 2006 Dec 1;364(3):243-7. Epub 2006 Sep 9. PMID:17011573 doi:http://dx.doi.org/10.1016/j.jmb.2006.09.011
↑ Bond CS, Kvaratskhelia M, Richard D, White MF, Hunter WN. Structure of Hjc, a Holliday junction resolvase, from Sulfolobus solfataricus. Proc Natl Acad Sci U S A. 2001 May 8;98(10):5509-14. Epub 2001 May 1. PMID:11331763 doi:10.1073/pnas.091613398

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hh1"

@@ Line 2: / Line 2: @@
 <StructureSection load='1hh1' size='340' side='right' caption='[[1hh1]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hh1]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HH1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hh1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HH1 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1hh1 RCSB], [http://www.ebi.ac.uk/pdbsum/1hh1 PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1hh1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hh1 RCSB], [http://www.ebi.ac.uk/pdbsum/1hh1 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/HJC_SULSO HJC_SULSO]] A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination; may have some degree of sequence preference in a mobile junction. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products. Can cleave all 4 strands 3 bases 3' of the junction center. Cleaves both mobile and immobile junctions. Modifies the structure of the 4-way DNA junction, a model Holliday junction structure. The protein forms multiple complexes with 4-way DNA, suggesting more than 1 homodimer can bind to each junction.<ref>PMID:10701121</ref> <ref>PMID:10736227</ref> <ref>PMID:10940317</ref> <ref>PMID:11709558</ref> <ref>PMID:17011573</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 23: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1hh1" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 30: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Sulfolobus solfataricus]]
+[[Category: Atcc 35091]]
 [[Category: Bond, C S]]
 [[Category: Hunter, W N]]

1hh1

From Proteopedia

Revision as of 23:53, 10 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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