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dc.contributor.authorFonner, Brittany A.
dc.contributor.authorTripet, Brian P.
dc.contributor.authorLui, Mengyao
dc.contributor.authorLei, Benfang
dc.contributor.authorCopie, Valerie
dc.date.accessioned2016-01-27T17:27:00Z
dc.date.available2016-01-27T17:27:00Z
dc.date.issued2013-05
dc.identifier.citationFonner, Brittany A., Brian P. Tripet, Mengyao Lui, Hui Zhu, Benfang Lei, and Valérie Copié. “1H, 13C, 15N Backbone and Side Chain NMR Resonance Assignments of the N-Terminal NEAr Iron Transporter Domain 1 (NEAT 1) of the Hemoglobin Receptor IsdB of Staphylococcus Aureus.” Biomol NMR Assign 8, no. 1 (May 18, 2013): 201–205. doi:10.1007/s12104-013-9483-5.en_US
dc.identifier.issn1874-2718
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/9521
dc.description.abstractStaphylococcus aureus is an opportunistic pathogen that causes skin and severe infections in mammals. Critical to S. aureus growth is its ability to scavenge iron from host cells. To this effect, S. aureus has evolved a sophisticated pathway to acquire heme from hemoglobin (Hb) as a preferred iron source. The pathway is comprised of nine iron-regulated surface determinant (Isd) proteins involved in heme capture, transport, and degradation. A key protein of the heme acquisition pathway is the surface-anchored hemoglobin receptor protein IsdB, which is comprised of two NEAr transporter (NEAT) domains that act in concert to bind Hb and extract heme for subsequent transfer to downstream acquisition pathway proteins. Despite significant advances in the structural knowledge of other Isd proteins, the structural mechanisms and molecular basis of the IsdB-mediated heme acquisition process are not well understood. In order to provide more insights into the mode of function of IsdB, we have initiated NMR structural studies of the first NEAT domain of IsdB (IsdBN1). Herein, we report the near complete 1H, 13C and 15N resonance assignments of backbone and side chain atoms, and the secondary structural topology of the 148-residue IsdB NEAT 1 domain. The NMR results are consistent with the presence of eight β-strands and one α-helix characteristic of an immunoglobulin-like fold observed in other NEAT domain family proteins. This work provides a solid framework to obtain atomic-level insights toward understanding how IsdB mediates IsdB-Hb protein–protein interactions critical for heme capture and transfer.en_US
dc.description.sponsorshipThis work was funded by the National Science Foundation, NSF grant MCB-0920312. The initial work on IsdBN1 in the Lei lab was funded in part by NIH grants GM103500-09 and AI095704. The NMR experiments were recorded at Montana State University on a DRX600 Bruker solution NMR spectrometer, purchased in part with funds from the NIH Shared Instrumentation Grant (SIG) (Grant Number 1S10-RR13878-01), and recently upgraded to an AVANCE III console and cryogenically cooled TCI probe (Grant Number 1S10-RR026659-01). Support for the Mass Spectrometry Facility has been provided by The Murdock Charitable trust, an NIH INBRE grant P20-RR-16455-08, and NIH Grants P20-RR-020185 and 1P20-RR-024237 from the NIH Center of Biomedical Research Excellence (CoBRE) Programs.en_US
dc.title¹H, ¹³C, ¹⁵N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureusen_US
dc.typeArticleen_US
mus.citation.extentfirstpage201en_US
mus.citation.extentlastpage205en_US
mus.citation.issue1en_US
mus.citation.journaltitleBiomolecular NMR Assignmentsen_US
mus.citation.volume8en_US
mus.identifier.categoryHealth & Medical Sciencesen_US
mus.identifier.doi10.1007/s12104-013-9483-5en_US
mus.relation.collegeCollege of Agricultureen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.contributor.orcidCopie, Valerie|0000-0002-2778-1463en_US


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