5H3N
Solution structure of human Gelsolin protein domain 1 at pH 7.3
Summary for 5H3N
| Entry DOI | 10.2210/pdb5h3n/pdb |
| Related | 5H3M |
| NMR Information | BMRB: 36027 |
| Descriptor | Gelsolin (1 entity in total) |
| Functional Keywords | gelsolin, structural protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 14973.82 |
| Authors | |
| Primary citation | Fan, J.S.,Goh, H.,Ding, K.,Xue, B.,Robinson, R.C.,Yang, D. Structural Basis for pH-mediated Regulation of F-actin Severing by Gelsolin Domain 1. Sci Rep, 7:45230-45230, 2017 Cited by PubMed Abstract: Six-domain gelsolin regulates actin structural dynamics through its abilities to sever, cap and uncap F-actin. These activities are modulated by various cellular parameters like Ca and pH. Until now, only the molecular activation mechanism of gelsolin by Ca has been understood relatively well. The fragment comprising the first domain and six residues from the linker region into the second domain has been shown to be similar to the full-length protein in F-actin severing activity in the absence of Ca at pH 5. To understand how this gelsolin fragment is activated for F-actin severing by lowering pH, we solved its NMR structures at both pH 7.3 and 5 in the absence of Ca and measured the pKa values of acidic amino acid residues and histidine residues. The overall structure and dynamics of the fragment are not affected significantly by pH. Nevertheless, local structural changes caused by protonation of His29 and Asp109 result in the activation on lowering the pH, and protonation of His151 directly effects filament binding since it resides in the gelsolin/actin interface. Mutagenesis studies support that His29, Asp109 and His151 play important roles in the pH-dependent severing activity of the gelsolin fragment. PubMed: 28349924DOI: 10.1038/srep45230 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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