6KG8
Solution structure of CaCohA2 from Clostridium acetobutylicum
Summary for 6KG8
| Entry DOI | 10.2210/pdb6kg8/pdb |
| Related | 6KG9 6KGC 6KGD 6KGE 6KGF |
| Descriptor | Probably cellulosomal scaffolding protein, secreted cellulose-binding and cohesin domain (1 entity in total) |
| Functional Keywords | cohesin, cellulosome, scaffolding, beta sandwitch, hydrolase |
| Biological source | Clostridium acetobutylicum ATCC 824 |
| Total number of polymer chains | 1 |
| Total formula weight | 16027.81 |
| Authors | |
| Primary citation | Yao, X.,Chen, C.,Wang, Y.,Dong, S.,Liu, Y.J.,Li, Y.,Cui, Z.,Gong, W.,Perrett, S.,Yao, L.,Lamed, R.,Bayer, E.A.,Cui, Q.,Feng, Y. Discovery and mechanism of a pH-dependent dual-binding-site switch in the interaction of a pair of protein modules. Sci Adv, 6:-, 2020 Cited by PubMed Abstract: Many important proteins undergo pH-dependent conformational changes resulting in "on-off" switches for protein function, which are essential for regulation of life processes and have wide application potential. Here, we report a pair of cellulosomal assembly modules, comprising a cohesin and a dockerin from , which interact together following a unique pH-dependent switch between two functional sites rather than on-off states. The two cohesin-binding sites on the dockerin are switched from one to the other at pH 4.8 and 7.5 with a 180° rotation of the bound dockerin. Combined analysis by nuclear magnetic resonance spectroscopy, crystal structure determination, mutagenesis, and isothermal titration calorimetry elucidates the chemical and structural mechanism of the pH-dependent switching of the binding sites. The pH-dependent dual-binding-site switch not only represents an elegant example of biological regulation but also provides a new approach for developing pH-dependent protein devices and biomaterials beyond an on-off switch for biotechnological applications. PubMed: 33097546DOI: 10.1126/sciadv.abd7182 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
