Linked Life Data

1992356

Source:http://linkedlifedata.com/resource/pubmed/id/1992356

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6309
pubmed:dateCreated
1991-3-11
pubmed:abstractText
Ferritin is important in iron homeostasis. Its twenty-four chains of two types, H and L, assemble as a hollow shell providing an iron-storage cavity. Ferritin molecules in cells containing high levels of iron tend to be rich in L chains, and may have a long-term storage function, whereas H-rich ferritins are more active in iron metabolism. The molecular basis for the greater activity of H-rich ferritins has until now been obscure, largely because the structure of H-chain ferritin has remained unknown owing to the difficulties in obtaining crystals ordered enough for X-ray crystallographic analysis. Here we report the three-dimensional structure of a human ferritin H-chain homopolymer. By genetically engineering a change in the sequence of the intermolecular contact region, we obtained crystals isomorphous with the homologous rat L ferritin and of high enough quality for X-ray diffraction analysis. The X-ray structure of human H ferritin shows a novel metal site embedded within each of its four-helix bundles and we suggest that ferroxidase activity associated with this site accounts for its rapid uptake of iron.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
349
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
541-4
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts.
pubmed:affiliation
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University, Sheffield, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't