1en7: Difference between revisions

Revision as of 01:02, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1en7.png

Template:STRUCTURE 1en7

ENDONUCLEASE VII (ENDOVII) FROM PHAGE T4ENDONUCLEASE VII (ENDOVII) FROM PHAGE T4

Template:ABSTRACT PUBMED 10075917

About this StructureAbout this Structure

1EN7 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

X-ray structure of T4 endonuclease VII: a DNA junction resolvase with a novel fold and unusual domain-swapped dimer architecture., Raaijmakers H, Vix O, Toro I, Golz S, Kemper B, Suck D, EMBO J. 1999 Mar 15;18(6):1447-58. PMID:10075917

Page seeded by OCA on Tue Jul 1 01:02:34 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1en7.jpg|left|200px]]
+{{Seed}}
+[[Image:1en7.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1en7|  PDB=1en7  |  SCENE=  }}
-'''ENDONUCLEASE VII (ENDOVII) FROM PHAGE T4'''
+===ENDONUCLEASE VII (ENDOVII) FROM PHAGE T4===
-==Overview==
+<!--
-Phage T4 endonuclease VII (Endo VII), the first enzyme shown to resolve Holliday junctions, recognizes a broad spectrum of DNA substrates ranging from branched DNAs to single base mismatches. We have determined the crystal structures of the Ca2+-bound wild-type and the inactive N62D mutant enzymes at 2.4 and 2.1 A, respectively. The Endo VII monomers form an elongated, highly intertwined molecular dimer exhibiting extreme domain swapping. The major dimerization elements are two pairs of antiparallel helices forming a novel 'four-helix cross' motif. The unique monomer fold, almost completely lacking beta-sheet structure and containing a zinc ion tetrahedrally coordinated to four cysteines, does not resemble any of the known junction-resolving enzymes, including the Escherichia coli RuvC and lambda integrase-type recombinases. The S-shaped dimer has two 'binding bays' separated by approximately 25 A which are lined by positively charged residues and contain near their base residues known to be essential for activity. These include Asp40 and Asn62, which function as ligands for the bound calcium ions. A pronounced bipolar charge distribution suggests that branched DNA substrates bind to the positively charged face with the scissile phosphates located near the divalent cations. A model for the complex with a four-way DNA junction is presented.
+The line below this paragraph, {{ABSTRACT_PUBMED_10075917}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10075917 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10075917}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Holliday junction]]
 [[Category: Resolvase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:18:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 01:02:34 2008''