CRYSTAL STRUCTURE OF BOVINE CU, ZN SOD TO 1.7 ANGSTROM (3 OF 3)

File:1e9p.gif


1e9p, resolution 1.70Å

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OverviewOverview

The structure of the catalytic site in one subunit of bovine CuZn, superoxide dismutase is shown to be highly variable. A series of crystal, structures at approximately 1.7 A have been determined using data, collected from different crystals. Several conformations are observed for, the copper site from one of the subunits. These conformations lie between, those expected for the Cu(II) and Cu(I) forms of the enzyme and may, represent a slow positional rearrangement of the Cu site during the, crystallisation process due to the presence of a trace reductant in the, mother liquor. These states perhaps indicate some functionally relevant, structural steps that ultimately result in the breakage of the imidazolate, bridge between the two metal sites.This behaviour is not observed for the, second ... [(full description)]

About this StructureAbout this Structure

1E9P is a [Protein complex] structure of sequences from [Bos taurus] with CU and ZN as [ligands]. Active as [Transferred entry: 1.13.11.1], with EC number [1.13.1.1]. Structure known Active Sites: CU1, CU2, CU3 and ZNB. Full crystallographic information is available from [OCA].

ReferenceReference

Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function., Hough MA, Strange RW, Hasnain SS, J Mol Biol. 2000 Nov 24;304(2):231-41. PMID:11080458

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