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Structural characterisation of the HT3 motif of the polyhistidine triad protein D from Streptococcus pneumoniae
- Source :
- FEBS Letters. 592:2341-2350
- Publication Year :
- 2018
- Publisher :
- Wiley, 2018.
-
Abstract
- The bacterium Streptococcus pneumoniae (the pneumococcus) is a major human pathogen that requires Zn2+ for its survival and virulence in the host environment. Polyhistidine triad protein D (PhtD) has a known role in pneumococcal Zn2+ homeostasis. However, the mechanistic basis of PhtD function remains unclear, partly due to a lack of structural information. Here, we determined the crystal structure of the fragment PhtD269-339 , containing the third Zn2+ -binding histidine triad (HT) motif of the protein. Analysis of the structure suggests that Zn2+ binding occurs at the surface of the protein and that all five HT motifs in the protein bind Zn2+ and share similar structures. These new structural insights aid in our understanding of how the Pht proteins facilitate pneumococcal Zn2+ acquisition.
- Subjects :
- Models, Molecular
inorganic chemicals
0301 basic medicine
Protein Conformation
030106 microbiology
Biophysics
Virulence
Human pathogen
Plasma protein binding
Crystallography, X-Ray
medicine.disease_cause
Biochemistry
03 medical and health sciences
Protein structure
Bacterial Proteins
Structural Biology
Catalytic Domain
Streptococcus pneumoniae
Genetics
medicine
Histidine
Protein Interaction Domains and Motifs
Molecular Biology
biology
Chemistry
Cell Biology
biology.organism_classification
3. Good health
Zinc
biological sciences
health occupations
bacteria
Homeostasis
Bacteria
Protein Binding
Subjects
Details
- ISSN :
- 18733468 and 00145793
- Volume :
- 592
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....c624fdd1a50ea2374284e3784adf2711