1h56
From Proteopedia
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STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF A NEW MAGNESIUM ION BINDING SITE NEAR TYR94 IN THE RESTRICTION ENDONUCLEASE PVUII
Overview
We have determined the crystal structure of the PvuII endonuclease in the, presence of Mg(2+). According to the structural data, divalent metal ion, binding in the PvuII subunits is highly asymmetric. The PvuII-Mg(2+), complex has two distinct metal ion binding sites, one in each monomer. One, site is formed by the catalytic residues Asp58 and Glu68, and has, extensive similarities to a catalytically important site found in all, structurally examined restriction endonucleases. The other binding site is, located in the other monomer, in the immediate vicinity of the hydroxyl, group of Tyr94; it has no analogy to metal ion binding sites found so far, in restriction endonucleases. To assign the number of metal ions involved, and to better understand the role of Mg(2+) binding to Tyr94 for ... [(full description)]
About this Structure
1H56 is a [Single protein] structure of sequence from [Proteus vulgaris] with MG as [ligand]. Active as [[1]], with EC number [3.1.21.4]. Full crystallographic information is available from [OCA].
Reference
Structural and biochemical characterization of a new Mg(2+) binding site near Tyr94 in the restriction endonuclease PvuII., Spyridaki A, Matzen C, Lanio T, Jeltsch A, Simoncsits A, Athanasiadis A, Scheuring-Vanamee E, Kokkinidis M, Pingoud A, J Mol Biol. 2003 Aug 8;331(2):395-406. PMID:12888347
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