We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1znv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1znv.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1znv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1znv| PDB=1znv | SCENE= }}
{{STRUCTURE_1znv| PDB=1znv | SCENE= }}
-
'''How a His-metal finger endonuclease ColE7 binds and cleaves DNA with a transition metal ion cofactor'''
+
===How a His-metal finger endonuclease ColE7 binds and cleaves DNA with a transition metal ion cofactor===
-
==Overview==
+
<!--
-
The nuclease domain of ColE7 (N-ColE7) contains an H-N-H motif that folds in a beta beta alpha-metal topology. Here we report the crystal structures of a Zn2+-bound N-ColE7 (H545E mutant) in complex with a 12-bp duplex DNA and a Ni2+-bound N-ColE7 in complex with the inhibitor Im7 at a resolution of 2.5 A and 2.0 A, respectively. Metal-dependent cleavage assays showed that N-ColE7 cleaves double-stranded DNA with a single metal ion cofactor, Ni2+, Mg2+, Mn2+, and Zn2+. ColE7 purified from Escherichia coli contains an endogenous zinc ion that was not replaced by Mg2+ at concentrations of &lt;25 mM, indicating that zinc is the physiologically relevant metal ion in N-ColE7 in host E. coli. In the crystal structure of N-ColE7/DNA complex, the zinc ion is directly coordinated to three histidines and the DNA scissile phosphate in a tetrahedral geometry. In contrast, Ni2+ is bound in N-ColE7 in two different modes, to four ligands (three histidines and one phosphate ion), or to five ligands with an additional water molecule. These data suggest that the divalent metal ion in the His-metal finger motif can be coordinated to six ligands, such as Mg2+ in I-PpoI, Serratia nuclease and Vvn, five ligands or four ligands, such as Ni2+ or Zn2+ in ColE7. Universally, the metal ion in the His-metal finger motif is bound to the DNA scissile phosphate and serves three roles during hydrolysis: polarization of the P-O bond for nucleophilic attack, stabilization of the phosphoanion transition state and stabilization of the cleaved product.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16434744}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16434744 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16434744}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Ni-binding]]
[[Category: Ni-binding]]
[[Category: Protein-protein complex]]
[[Category: Protein-protein complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:51:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:07:54 2008''

Revision as of 17:07, 28 July 2008

Image:1znv.png

Template:STRUCTURE 1znv

How a His-metal finger endonuclease ColE7 binds and cleaves DNA with a transition metal ion cofactor

Template:ABSTRACT PUBMED 16434744

About this Structure

1ZNV is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structural analysis and metal-dependent stability and activity studies of the ColE7 endonuclease domain in complex with DNA/Zn2+ or inhibitor/Ni2+., Doudeva LG, Huang H, Hsia KC, Shi Z, Li CL, Shen Y, Cheng YS, Yuan HS, Protein Sci. 2006 Feb;15(2):269-80. PMID:16434744

Page seeded by OCA on Mon Jul 28 20:07:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1znv"
Personal tools