5DBL
Crystal structure of the Staphylococcus aureus SasG E1-G52 Y625W mutant
Summary for 5DBL
| Entry DOI | 10.2210/pdb5dbl/pdb |
| Related | 3TIP |
| Descriptor | Surface protein G (2 entities in total) |
| Functional Keywords | sasg, biofilm, staphylococcus aureus, structural protein |
| Biological source | Staphylococcus aureus |
| Cellular location | Secreted, cell wall ; Peptidoglycan-anchor : Q2G2B2 |
| Total number of polymer chains | 1 |
| Total formula weight | 14516.24 |
| Authors | Whelan, F.,Potts, J.R. (deposition date: 2015-08-21, release date: 2016-09-28, Last modification date: 2024-01-10) |
| Primary citation | Gruszka, D.T.,Mendonca, C.A.,Paci, E.,Whelan, F.,Hawkhead, J.,Potts, J.R.,Clarke, J. Disorder drives cooperative folding in a multidomain protein. Proc.Natl.Acad.Sci.USA, 113:11841-11846, 2016 Cited by PubMed Abstract: Many human proteins contain intrinsically disordered regions, and disorder in these proteins can be fundamental to their function-for example, facilitating transient but specific binding, promoting allostery, or allowing efficient posttranslational modification. SasG, a multidomain protein implicated in host colonization and biofilm formation in Staphylococcus aureus, provides another example of how disorder can play an important role. Approximately one-half of the domains in the extracellular repetitive region of SasG are intrinsically unfolded in isolation, but these E domains fold in the context of their neighboring folded G5 domains. We have previously shown that the intrinsic disorder of the E domains mediates long-range cooperativity between nonneighboring G5 domains, allowing SasG to form a long, rod-like, mechanically strong structure. Here, we show that the disorder of the E domains coupled with the remarkable stability of the interdomain interface result in cooperative folding kinetics across long distances. Formation of a small structural nucleus at one end of the molecule results in rapid structure formation over a distance of 10 nm, which is likely to be important for the maintenance of the structural integrity of SasG. Moreover, if this normal folding nucleus is disrupted by mutation, the interdomain interface is sufficiently stable to drive the folding of adjacent E and G5 domains along a parallel folding pathway, thus maintaining cooperative folding. PubMed: 27698144DOI: 10.1073/pnas.1608762113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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