| Title |
Solution structure of the major (Spy0128) and minor (Spy0125 and Spy0130) pili subunits from Streptococcus pyogenes
|
|---|---|
| Published in |
European Biophysics Journal, March 2009
|
| DOI | 10.1007/s00249-009-0432-2 |
| Pubmed ID | |
| Authors |
Alexandra S. Solovyova, Jonathan A. Pointon, Paul R. Race, Wendy D. Smith, Michael A. Kehoe, Mark J. Banfield |
| Abstract |
Adhesion of the serotype M1 Streptococcus pyogenes strain SF370 to human tonsil explants and cultured keratinocytes requires extended polymeric surface structures called pili. In this important human pathogen, pili are assembled from three protein subunits: Spy0125, Spy0128 and Spy0130 through the action of sortase enzymes. For this study, the structural properties of these pili proteins have been investigated in solution. Spy0125 and Spy0128 display characteristics of globular, folded proteins. Circular dichroism suggests a largely beta-sheet composition for Spy0128 and Spy0125; Spy0130 appears to contain little secondary structure. Each of the proteins adopts a monodisperse, monomeric state in solution as assessed by analytical ultracentrifugation. Further, small-angle X-ray scattering curves for Spy0125, Spy0128 and Spy0130 suggest each protein adopts an elongated shape, likely comprised of two domains, with similar maximal dimensions. Based on the scattering data, dummy atom models of each of the pili subunits have been reconstructed ab initio. This study provides the first insights into the structure of Streptococcus pyogenes minor pili subunits, and possible implications for protein function are discussed. |
Mendeley readers
The data shown below were compiled from readership statistics for 24 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| India | 1 | 4% |
| Unknown | 23 | 96% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 6 | 25% |
| Student > Ph. D. Student | 4 | 17% |
| Student > Bachelor | 3 | 13% |
| Student > Doctoral Student | 2 | 8% |
| Student > Master | 2 | 8% |
| Other | 3 | 13% |
| Unknown | 4 | 17% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 8 | 33% |
| Biochemistry, Genetics and Molecular Biology | 3 | 13% |
| Chemistry | 3 | 13% |
| Chemical Engineering | 1 | 4% |
| Computer Science | 1 | 4% |
| Other | 4 | 17% |
| Unknown | 4 | 17% |
Attention Score in Context
This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 26 December 2017.
All research outputs
#7,454,427
of 22,789,566 outputs
Outputs from European Biophysics Journal
#101
of 490 outputs
Outputs of similar age
#37,600
of 106,971 outputs
Outputs of similar age from European Biophysics Journal
#3
of 10 outputs
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