View : 13 Download: 0

The Crystal Structure of Ferritin from Helicobacter pylori Reveals Unusual Conformational Changes for Iron Uptake

Title
The Crystal Structure of Ferritin from Helicobacter pylori Reveals Unusual Conformational Changes for Iron Uptake
Authors
Cho K.J.Shin H.J.Lee J.-H.Kim K.-J.Park S.S.Lee Y.Lee C.Kim K.H.
Ewha Authors
이영미
SCOPUS Author ID
이영미scopus
Issue Date
2009
Journal Title
Journal of Molecular Biology
ISSN
0022-2836JCR Link
Citation
vol. 390, no. 1, pp. 83 - 98
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The crystal structure of recombinant ferritin from Helicobacter pylori has been determined in its apo, low-iron-bound, intermediate, and high-iron-bound states. Similar to other members of the ferritin family, the bacterial ferritin assembles as a spherical protein shell of 24 subunits, each of which folds into a four-α-helix bundle. Significant conformational changes were observed at the BC loop and the entrance of the 4-fold symmetry channel in the intermediate and high-iron-bound states, whereas no change was found in the apo and low-iron-bound states. The imidazole rings of His149 at the channel entrance undergo conformational changes that bear resemblance to heme configuration and are directly coupled to axial translocation of Fe ions through the 4-fold channel. Our results provide the first structural evidence of the translocation of Fe ions through the 4-fold channel in prokaryotes and the transition from a protein-dominated process to a mineral-surface-dominated process during biomineralization. © 2009 Elsevier Ltd. All rights reserved.
DOI
10.1016/j.jmb.2009.04.078
Appears in Collections:
자연과학대학 > 화학·나노과학전공 > Journal papers
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE