The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin
详细信息 查看全文
- 作者：Megan Sjodt1 ; 2 ; 3 ; Ramsay Macdonald1 ; 2 ; 3 ; Thomas Spirig1 ; Albert H. Chan1 ; 2 ; 3 ; Claire F. Dickson5 ; Marian Fabian4 ; John S. Olson4 ; David A. Gell5 ; Robert T. Clubb1 ; 2 ; 3 ; rclubb@mbi.ucla.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Isd ; iron-regulated surface determinant ; PRE ; paramagnetic relaxation enhancement ; RDC ; residual dipolar coupling ; HSQC ; heteronuclear single quantum coherence ; NOE ; nuclear Overhauser effect ; NOESY ; NOE spectroscopy ; SAXS ; small-angle X-ray scattering
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：27 March 2016
- 年：2016
- 卷：428
- 期：6
- 页码：1107-1129
- 全文大小：2370 K
文摘
- •
S. aureus procures heme-iron from hemoglobin using tri-domain receptors.
- •
PRE NMR is used to model the 38.8-kDa receptor structure.
- •
Ensemble calculations were used to estimate domain mobility within the receptor.
- •
Receptor may trigger heme release from human hemoglobin by perturbing its F helix.
- •
This study reveals how Gram-positive bacteria acquire iron from human hemoglobin.