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1v15

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[[Image:1v15.gif|left|200px]]
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{{Seed}}
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[[Image:1v15.png|left|200px]]
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{{STRUCTURE_1v15| PDB=1v15 | SCENE= }}
{{STRUCTURE_1v15| PDB=1v15 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE COLICIN E9, MUTANT HIS103ALA, IN COMPLEX WITH ZN+2 AND DSDNA (RESOLUTION 2.4A)'''
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===CRYSTAL STRUCTURE OF THE COLICIN E9, MUTANT HIS103ALA, IN COMPLEX WITH ZN+2 AND DSDNA (RESOLUTION 2.4A)===
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==Overview==
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Controversy surrounds the metal-dependent mechanism of H-N-H endonucleases, enzymes involved in a variety of biological functions, including intron homing and DNA repair. To address this issue we determined the crystal structures for complexes of the H-N-H motif containing bacterial toxin colicin E9 with Zn(2+), Zn(2+).DNA, and Mg(2+).DNA. The structures show that the rigid V-shaped architecture of the active site does not undergo any major conformational changes on binding to the minor groove of DNA and that the same interactions are made to the nucleic acid regardless of which metal ion is bound to the enzyme. The scissile phosphate contacts the single metal ion of the motif through distortion of the DNA brought about by the insertion of the Arg-96-Glu-100 salt bridge into the minor groove and a network of contacts to the DNA phosphate backbone that straddle the metal site. The Mg(2+)-bound structure reveals an unusual coordination scheme involving two H-N-H histidine residues, His-102 and His-127. The mechanism of DNA cleavage is likely related to that of other single metal ion-dependent endonucleases, such as I-PpoI and Vvn, although in these enzymes the single alkaline earth metal ion is coordinated by oxygen-bearing amino acids. The structures also provide a rationale as to why H-N-H endonucleases are inactive in the presence of Zn(2+) but active with other transition metal ions such as Ni(2+). This is because of coordination of the Zn(2+) ion through a third histidine, His-131. "Active" transition metal ions are those that bind more weakly to the H-N-H motif because of the disengagement of His-131, which we suggest allows a water molecule to complete the catalytic cycle.
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The line below this paragraph, {{ABSTRACT_PUBMED_15190054}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15190054 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15190054}}
==About this Structure==
==About this Structure==
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[[Category: Homing endonuclease]]
[[Category: Homing endonuclease]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:57:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:06:39 2008''

Revision as of 09:06, 29 July 2008

Image:1v15.png

Template:STRUCTURE 1v15

CRYSTAL STRUCTURE OF THE COLICIN E9, MUTANT HIS103ALA, IN COMPLEX WITH ZN+2 AND DSDNA (RESOLUTION 2.4A)

Template:ABSTRACT PUBMED 15190054

About this Structure

1V15 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure-based analysis of the metal-dependent mechanism of H-N-H endonucleases., Mate MJ, Kleanthous C, J Biol Chem. 2004 Aug 13;279(33):34763-9. Epub 2004 Jun 8. PMID:15190054

Page seeded by OCA on Tue Jul 29 12:06:39 2008

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