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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sun, Xuesong Ge, Ruiguang Zhang, Dongmei Sun, Hongzhe He, Qing-Yu |
| Description | Country affiliation: China Author Affiliation: Sun X ( Institute of Life and Health Engineering/National Engineering and Research Center of Genetic Medicine, Jinan University, Guangzhou, 510632, China.) |
| 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 dissociates 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. |
| File Format | HTM / HTML |
| ISSN | 09498257 |
| Issue Number | 8 |
| Volume Number | 15 |
| e-ISSN | 14321327 |
| Journal | JBIC Journal of Biological Inorganic Chemistry |
| Language | English |
| Publisher | Springer |
| Publisher Date | 2010-11-01 |
| Publisher Place | Germany |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Bacterial Outer Membrane Proteins Metabolism Membrane Transport Proteins Streptococcus Pyogenes Enzymology Chemistry Binding Sites Circular Dichroism Heme Protein Structure, Secondary Spectrometry, Fluorescence Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Inorganic Chemistry |
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