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3D morphology of the human hepatic ferritin mineral core: new evidence for a subunit structure revealed by single particle analysis of HAADF-STEM images.

Abstract：

:Ferritin, the major iron storage protein, has dual functions; it sequesters redox activity of intracellular iron and facilitates iron turn-over. Here we present high angle annular dark field (HAADF) images from individual hepatic ferritin cores within tissue sections, these images were obtained using spherical aberration corrected scanning transmission electron microscopy (STEM) under controlled electron fluence. HAADF images of the cores suggest a cubic morphology and a polycrystalline (ferrihydrite) subunit structure that is not evident in equivalent bright field images. By calibrating contrast levels in the HAADF images using quantitative electron energy loss spectroscopy, we have estimated the absolute iron content in any one core, and produced a three dimensional reconstruction of the average core morphology. The core is composed of up to eight subunits, consistent with the eight channels in the protein shell that deliver iron to the central cavity. We find no evidence of a crystallographic orientation relationship between core subunits. Our results confirm that the ferritin protein shell acts as a template for core morphology and within the core, small (approximately 2 nm), surface-disordered ferrihydrite subunits connect to leave a low density centre and a high surface area that would allow rapid turn-over of iron in biological systems.

journal_name

J Struct Biol

journal_title

Journal of structural biology

authors

Pan YH,Sader K,Powell JJ,Bleloch A,Gass M,Trinick J,Warley A,Li A,Brydson R,Brown A

doi

10.1016/j.jsb.2008.12.001

subject

Has Abstract

pub_date

2009-04-01 00:00:00

pages

22-31

issue

1

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(08)00294-3

journal_volume

166

pub_type

杂志文章

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