2cn6

From Proteopedia

Revision as of 06:20, 30 October 2007

RECOMBINANT HUMAN H FERRITIN, K86Q AND E107D MUTANT, SOAKED WITH ZN IONS

Overview

Ferritins are a family of proteins distributed widely in nature. In, bacterial, plant, and animal cells, ferritin appears to serve as a, soluble, bioavailable, and non-toxic form of iron provider. Ferritins from, animal sources are heteropolymers composed of two types of subunit, H and, L, which differ mainly by the presence (H) or absence (L) of active, ferroxidase centres. We report the crystallographic structures of four, human H apoferritin variants at a resolution of up to 1.5 Angstrom., Crystal derivatives using Zn(II) as redox-stable alternative for Fe(II), allows us to characterize the different metal-binding sites. The, ferroxidase centre, which is composed of sites A and B, binds metal with a, preference for the A site. In addition, distinct Zn(II)-binding sites were, found in ... [(full description)]

About this Structure

2CN6 is a [Single protein] structure of sequence from [Homo sapiens] with ZN, CA and GOL as [ligands]. Active as [Oxidoreductase], with EC number [1.16.3.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites., Toussaint L, Bertrand L, Hue L, Crichton RR, Declercq JP, J Mol Biol. 2007 Jan 12;365(2):440-52. Epub 2006 Oct 7. PMID:17070541

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