1lb3

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1lb3, resolution 1.21Å

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Structure of recombinant mouse L chain ferritin at 1.2 A resolution

Overview

The first ferritin structure refined at the atomic level has been achieved, on recombinant mouse L-chain apoferritin (rMoLF) crystals. These latter, diffract to 1.2 A resolution under cryogenic conditions. When cryo-cooling, the sample, the thermal disorder usually observed at room temperature is, reduced and the low-temperature structure reveals several details, concerning the protein putative active sites and their properties. Within, the pores built up by the molecular three-fold symmetry axes, the iron, entry route to the ferritin cavity, residues H118, D131 and E134, exhibit, alternate conformations associated with the binding of partially hydrated, cadmium ions, a metal used as a crystallization agent. At the mineral, ferrihydrite nucleation center, the electron density maps ... [(full description)]

About this Structure

1LB3 is a [Single protein] structure of sequence from [Mus musculus] with SO4, CD and GOL as [ligands]. Structure known Active Sites: NCL, SS1, SS2 and SS3. Full crystallographic information is available from [OCA].

Reference

Structural description of the active sites of mouse L-chain ferritin at 1.2 A resolution., Granier T, Langlois d'Estaintot B, Gallois B, Chevalier JM, Precigoux G, Santambrogio P, Arosio P, J Biol Inorg Chem. 2003 Jan;8(1-2):105-11. Epub 2002 Sep 6. PMID:12459904

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