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Article: Iron-containing lipoprotein SiaA in SiaABC, the primary heme transporter of Streptococcus pyogenes

TitleIron-containing lipoprotein SiaA in SiaABC, the primary heme transporter of Streptococcus pyogenes
Authors
Issue Date2010
PublisherSpringer 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?
AbstractThe 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 Identifierhttp://hdl.handle.net/10722/168493
ISSN
2015 Impact Factor: 2.495
2015 SCImago Journal Rankings: 0.882
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSun, Xen_US
dc.contributor.authorGe, Ren_US
dc.contributor.authorZhang, Den_US
dc.contributor.authorSun, Hen_US
dc.contributor.authorHe, QYen_US
dc.date.accessioned2012-10-08T03:19:36Z-
dc.date.available2012-10-08T03:19:36Z-
dc.date.issued2010en_US
dc.identifier.citationJournal Of Biological Inorganic Chemistry, 2010, v. 15 n. 8, p. 1265-1273en_US
dc.identifier.issn0949-8257en_US
dc.identifier.urihttp://hdl.handle.net/10722/168493-
dc.description.abstractThe 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.languageengen_US
dc.publisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00775/index.htmen_US
dc.relation.ispartofJournal of Biological Inorganic Chemistryen_US
dc.subject.meshBacterial Outer Membrane Proteins - Chemistry - Metabolismen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCircular Dichroismen_US
dc.subject.meshHeme - Chemistry - Metabolismen_US
dc.subject.meshMembrane Transport Proteins - Chemistry - Metabolismen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.subject.meshSpectrometry, Fluorescenceen_US
dc.subject.meshStreptococcus Pyogenes - Enzymologyen_US
dc.titleIron-containing lipoprotein SiaA in SiaABC, the primary heme transporter of Streptococcus pyogenesen_US
dc.typeArticleen_US
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_US
dc.identifier.authoritySun, H=rp00777en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/s00775-010-0684-4en_US
dc.identifier.pmid20607329-
dc.identifier.scopuseid_2-s2.0-78649934102en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-78649934102&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume15en_US
dc.identifier.issue8en_US
dc.identifier.spage1265en_US
dc.identifier.epage1273en_US
dc.identifier.isiWOS:000285264900010-
dc.publisher.placeGermanyen_US
dc.identifier.scopusauthoridSun, X=35799316500en_US
dc.identifier.scopusauthoridGe, R=7005525090en_US
dc.identifier.scopusauthoridZhang, D=37059911500en_US
dc.identifier.scopusauthoridSun, H=7404827446en_US
dc.identifier.scopusauthoridHe, QY=34770287900en_US
dc.identifier.citeulike7495161-

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