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- Publisher Website: 10.1007/s00775-010-0684-4
- Scopus: eid_2-s2.0-78649934102
- PMID: 20607329
- WOS: WOS:000285264900010
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Article: Iron-containing lipoprotein SiaA in SiaABC, the primary heme transporter of Streptococcus pyogenes
Title | Iron-containing lipoprotein SiaA in SiaABC, the primary heme transporter of Streptococcus pyogenes |
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Authors | |
Keywords | Heme transport Heme-binding protein Streptococcus pyogenes |
Issue Date | 2010 |
Publisher | Springer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00775/index.htm |
Citation | Journal Of Biological Inorganic Chemistry, 2010, v. 15 n. 8, p. 1265-1273 How to Cite? |
Abstract | The cell-surface lipoprotein SiaA, a component of the SiaABC transporter, acts as the primary receptor for heme in the infamous human pathogen Streptococcus pyogenes. However, little is known about the molecular mechanism of heme binding and release as well as the role of heme-binding ligands that contribute to the uptake of heme into the pathogenic bacteria. The present report aims to clarify the coordination properties of heme iron in SiaA. By substitution of either Met79 or His229 with alanine, the mutant M79A and H229A proteins display significantly decreased heme-binding affinity and substantially increased heme-release rates, as compared with wild-type SiaA protein. Both fluorescence and circular dichroism spectra indicated that heme binding results in alterations in the secondary structure of the protein. Heme release from SiaA is a stepwise process in which heme disassociates firstly from Met79 and then from His229 with distinct conformational changes. His229 may serve as an anchor for heme binding in SiaA and thus may play a major role in the stability of the coordination between heme and the protein. © 2010 SBIC. |
Persistent Identifier | http://hdl.handle.net/10722/168493 |
ISSN | 2023 Impact Factor: 2.7 2023 SCImago Journal Rankings: 0.543 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Sun, X | en_US |
dc.contributor.author | Ge, R | en_US |
dc.contributor.author | Zhang, D | en_US |
dc.contributor.author | Sun, H | en_US |
dc.contributor.author | He, QY | en_US |
dc.date.accessioned | 2012-10-08T03:19:36Z | - |
dc.date.available | 2012-10-08T03:19:36Z | - |
dc.date.issued | 2010 | en_US |
dc.identifier.citation | Journal Of Biological Inorganic Chemistry, 2010, v. 15 n. 8, p. 1265-1273 | en_US |
dc.identifier.issn | 0949-8257 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/168493 | - |
dc.description.abstract | The cell-surface lipoprotein SiaA, a component of the SiaABC transporter, acts as the primary receptor for heme in the infamous human pathogen Streptococcus pyogenes. However, little is known about the molecular mechanism of heme binding and release as well as the role of heme-binding ligands that contribute to the uptake of heme into the pathogenic bacteria. The present report aims to clarify the coordination properties of heme iron in SiaA. By substitution of either Met79 or His229 with alanine, the mutant M79A and H229A proteins display significantly decreased heme-binding affinity and substantially increased heme-release rates, as compared with wild-type SiaA protein. Both fluorescence and circular dichroism spectra indicated that heme binding results in alterations in the secondary structure of the protein. Heme release from SiaA is a stepwise process in which heme disassociates firstly from Met79 and then from His229 with distinct conformational changes. His229 may serve as an anchor for heme binding in SiaA and thus may play a major role in the stability of the coordination between heme and the protein. © 2010 SBIC. | en_US |
dc.language | eng | en_US |
dc.publisher | Springer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00775/index.htm | en_US |
dc.relation.ispartof | Journal of Biological Inorganic Chemistry | en_US |
dc.subject | Heme transport | - |
dc.subject | Heme-binding protein | - |
dc.subject | Streptococcus pyogenes | - |
dc.subject.mesh | Bacterial Outer Membrane Proteins - Chemistry - Metabolism | en_US |
dc.subject.mesh | Binding Sites | en_US |
dc.subject.mesh | Circular Dichroism | en_US |
dc.subject.mesh | Heme - Chemistry - Metabolism | en_US |
dc.subject.mesh | Membrane Transport Proteins - Chemistry - Metabolism | en_US |
dc.subject.mesh | Protein Structure, Secondary | en_US |
dc.subject.mesh | Spectrometry, Fluorescence | en_US |
dc.subject.mesh | Streptococcus Pyogenes - Enzymology | en_US |
dc.title | Iron-containing lipoprotein SiaA in SiaABC, the primary heme transporter of Streptococcus pyogenes | en_US |
dc.type | Article | en_US |
dc.identifier.email | Sun, H:hsun@hkucc.hku.hk | en_US |
dc.identifier.authority | Sun, H=rp00777 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1007/s00775-010-0684-4 | en_US |
dc.identifier.pmid | 20607329 | - |
dc.identifier.scopus | eid_2-s2.0-78649934102 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-78649934102&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 15 | en_US |
dc.identifier.issue | 8 | en_US |
dc.identifier.spage | 1265 | en_US |
dc.identifier.epage | 1273 | en_US |
dc.identifier.isi | WOS:000285264900010 | - |
dc.publisher.place | Germany | en_US |
dc.identifier.scopusauthorid | Sun, X=35799316500 | en_US |
dc.identifier.scopusauthorid | Ge, R=7005525090 | en_US |
dc.identifier.scopusauthorid | Zhang, D=37059911500 | en_US |
dc.identifier.scopusauthorid | Sun, H=7404827446 | en_US |
dc.identifier.scopusauthorid | He, QY=34770287900 | en_US |
dc.identifier.citeulike | 7495161 | - |
dc.identifier.issnl | 0949-8257 | - |