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Article: Crystal structure and metal binding properties of the lipoprotein MtsA, responsible for iron transport in Streptococcus pyogenes

TitleCrystal structure and metal binding properties of the lipoprotein MtsA, responsible for iron transport in Streptococcus pyogenes
Authors
Issue Date2009
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistry
Citation
Biochemistry, 2009, v. 48 n. 26, p. 6184-6190 How to Cite?
AbstractAn ability to acquire iron is essential for the viability and growth of almost all organisms and in pathogenic bacteria is strongly correlated with virulence. The cell surface lipoprotein MtsA, a component of the MtsABC transporter of Streptococcus pyogenes, acts as the primary receptor for inorganic iron by this significant human pathogen. Iron is bound as Fe 2+, with the participation of bicarbonate. The crystal structure of MtsA has been determined and refined at 1.8 Å resolution (R=0.167, and Rfree=0.194). MtsA has the classic bacterial metal binding receptor (MBR) fold, with the Fe2+ ion bound to the side chains of His68, His140, Glu206, and Asp281, at a totally enclosed site between the two domains of the protein. The absence of bicarbonate from the binding site suggests that it is displaced during the final stages of metal binding. Both the fold and metal binding site are most similar to those of the manganese receptors PsaA and MntC, consistent with the similar coordination requirements of Fe2+ and Mn2+. Binding studies confirm a 10-fold preference for Fe 2+ over Mn2+, although both may be carried in vivo. Mutational analysis of the binding site shows that His140 is critical for a fully functional binding site but that Glu206 is dispensable. The crystal structure explains the distinct roles of these ligands and also reveals potential secondary binding sites that may explain the binding behavior of MtsA for metal ions other than Fe2+. © 2009 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/69054
ISSN
2015 Impact Factor: 2.876
2015 SCImago Journal Rankings: 1.769
ISI Accession Number ID
Funding AgencyGrant Number
Health Research Council of New Zealand
Chang-Jiang Scholars Program 2007
China National Science Foundation20871057
Research CouncilHE722702
HKU751205
Funding Information:

This work was supported by funding from the Health Research Council of New Zealand (to E.N.B.), the Chang-Jiang Scholars Program 2007, "211" Projects, and China National Science Foundation Grant 20871057 (to Q.-Y.H.), and Research Council Grants HE722702 M and HKU751205 M (to Q.-Y.H. and H.S.).

References

 

DC FieldValueLanguage
dc.contributor.authorSun, Xen_HK
dc.contributor.authorBaker, HMen_HK
dc.contributor.authorGe, Ren_HK
dc.contributor.authorSun, Hen_HK
dc.contributor.authorHe, QYen_HK
dc.contributor.authorBaker, ENen_HK
dc.date.accessioned2010-09-06T06:10:07Z-
dc.date.available2010-09-06T06:10:07Z-
dc.date.issued2009en_HK
dc.identifier.citationBiochemistry, 2009, v. 48 n. 26, p. 6184-6190en_HK
dc.identifier.issn0006-2960en_HK
dc.identifier.urihttp://hdl.handle.net/10722/69054-
dc.description.abstractAn ability to acquire iron is essential for the viability and growth of almost all organisms and in pathogenic bacteria is strongly correlated with virulence. The cell surface lipoprotein MtsA, a component of the MtsABC transporter of Streptococcus pyogenes, acts as the primary receptor for inorganic iron by this significant human pathogen. Iron is bound as Fe 2+, with the participation of bicarbonate. The crystal structure of MtsA has been determined and refined at 1.8 Å resolution (R=0.167, and Rfree=0.194). MtsA has the classic bacterial metal binding receptor (MBR) fold, with the Fe2+ ion bound to the side chains of His68, His140, Glu206, and Asp281, at a totally enclosed site between the two domains of the protein. The absence of bicarbonate from the binding site suggests that it is displaced during the final stages of metal binding. Both the fold and metal binding site are most similar to those of the manganese receptors PsaA and MntC, consistent with the similar coordination requirements of Fe2+ and Mn2+. Binding studies confirm a 10-fold preference for Fe 2+ over Mn2+, although both may be carried in vivo. Mutational analysis of the binding site shows that His140 is critical for a fully functional binding site but that Glu206 is dispensable. The crystal structure explains the distinct roles of these ligands and also reveals potential secondary binding sites that may explain the binding behavior of MtsA for metal ions other than Fe2+. © 2009 American Chemical Society.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistryen_HK
dc.relation.ispartofBiochemistryen_HK
dc.subject.meshBacterial Proteins - chemistry - genetics - metabolism-
dc.subject.meshIron - metabolism-
dc.subject.meshLipoproteins - chemistry - genetics - metabolism-
dc.subject.meshMetals - metabolism-
dc.subject.meshStreptococcus pyogenes - chemistry-
dc.titleCrystal structure and metal binding properties of the lipoprotein MtsA, responsible for iron transport in Streptococcus pyogenesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0006-2960&volume=48&issue=26&spage=6168&epage=6190&date=2009&atitle=Crystal+structure+and+metal+binding+properties+of+the+lipoprotein+MtsA,+responsible+for+iron+transport+in+Streptococcus+pyogenesen_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/bi900552cen_HK
dc.identifier.pmid19463017-
dc.identifier.scopuseid_2-s2.0-67650092049en_HK
dc.identifier.hkuros163894en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-67650092049&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume48en_HK
dc.identifier.issue26en_HK
dc.identifier.spage6184en_HK
dc.identifier.epage6190en_HK
dc.identifier.isiWOS:000267609100017-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridSun, X=8906547400en_HK
dc.identifier.scopusauthoridBaker, HM=7402620669en_HK
dc.identifier.scopusauthoridGe, R=7005525090en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.scopusauthoridHe, QY=34770287900en_HK
dc.identifier.scopusauthoridBaker, EN=7401660725en_HK
dc.identifier.citeulike5070547-

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