File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Iron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe

TitleIron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe
Authors
Issue Date2012
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/srep/index.html
Citation
Scientific Reports, 2012, v. 2, p. Article no. 999 How to Cite?
AbstractHuman serum transferrin (hTF) binds Fe(III) tightly but reversibly, and delivers it to cells via a receptor-mediated endocytosis process. The metal-binding and release result in significant conformational changes of the protein. Here, we report the crystal structures of diferric-hTF (Fe N Fe C-hTF) and bismuth-bound hTF (Bi N Fe C-hTF) at 2.8 and 2.4 Å resolutions respectively. Notably, the N-lobes of both structures exhibit unique 'partially-opened' conformations between those of the apo-hTF and holo-hTF. Fe(III) and Bi(III) in the N-lobe coordinate to, besides anions, only two (Tyr95 and Tyr188) and one (Tyr188) tyrosine residues, respectively, in contrast to four residues in the holo-hTF. The C-lobe of both structures are fully closed with iron coordinating to four residues and a carbonate. The structures of hTF observed here represent key conformers captured in the dynamic nature of the transferrin family proteins and provide a structural basis for understanding the mechanism of metal uptake and release in transferrin families. © 2012 Macmillan Publishers Limited. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/184478
ISSN
2015 Impact Factor: 5.228
2015 SCImago Journal Rankings: 2.073
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYang, N-
dc.contributor.authorZhang, H-
dc.contributor.authorWang, M-
dc.contributor.authorHao, Q-
dc.contributor.authorSun, H-
dc.date.accessioned2013-07-15T09:49:08Z-
dc.date.available2013-07-15T09:49:08Z-
dc.date.issued2012-
dc.identifier.citationScientific Reports, 2012, v. 2, p. Article no. 999-
dc.identifier.issn2045-2322-
dc.identifier.urihttp://hdl.handle.net/10722/184478-
dc.description.abstractHuman serum transferrin (hTF) binds Fe(III) tightly but reversibly, and delivers it to cells via a receptor-mediated endocytosis process. The metal-binding and release result in significant conformational changes of the protein. Here, we report the crystal structures of diferric-hTF (Fe N Fe C-hTF) and bismuth-bound hTF (Bi N Fe C-hTF) at 2.8 and 2.4 Å resolutions respectively. Notably, the N-lobes of both structures exhibit unique 'partially-opened' conformations between those of the apo-hTF and holo-hTF. Fe(III) and Bi(III) in the N-lobe coordinate to, besides anions, only two (Tyr95 and Tyr188) and one (Tyr188) tyrosine residues, respectively, in contrast to four residues in the holo-hTF. The C-lobe of both structures are fully closed with iron coordinating to four residues and a carbonate. The structures of hTF observed here represent key conformers captured in the dynamic nature of the transferrin family proteins and provide a structural basis for understanding the mechanism of metal uptake and release in transferrin families. © 2012 Macmillan Publishers Limited. All rights reserved.-
dc.languageeng-
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/srep/index.html-
dc.relation.ispartofScientific Reports-
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.titleIron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe-
dc.typeArticle-
dc.identifier.emailYang, N: yangnan@hku.hk-
dc.identifier.emailZhang, H: hzhang20@hku.hk-
dc.identifier.emailHao, Q: qhao@hku.hk-
dc.identifier.emailSun, H: hsun@hku.hk-
dc.identifier.authorityZhang, H=rp00306-
dc.identifier.authorityHao, Q=rp01332-
dc.identifier.authoritySun, H=rp00777-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1038/srep00999-
dc.identifier.pmid23256035-
dc.identifier.pmcidPMC3525939-
dc.identifier.scopuseid=2-s2.0-84871947083-
dc.identifier.hkuros215978-
dc.identifier.volume2-
dc.identifier.spageArticle no. 999-
dc.identifier.epageArticle no. 999-
dc.identifier.isiWOS:000312489900002-
dc.publisher.placeUnited Kingdom-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats