1v14
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CRYSTAL STRUCTURE OF THE COLICIN E9, MUTANT HIS103ALA, IN COMPLEX WITH MG+2 AND DSDNA (RESOLUTION 2.9A)
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
1V14 is a [Single protein] structure of sequence from [Escherichia coli] with MG as [ligand]. Active as [Deoxyribonuclease I], with EC number [3.1.21.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
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
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