8C5V
Chemotaxis core signalling unit from E protein lysed E. coli cells
Summary for 8C5V
Entry DOI | 10.2210/pdb8c5v/pdb |
EMDB information | 15641 15642 15643 |
Descriptor | Chemotaxis protein CheA, Chemotaxis protein CheW, Methyl-accepting chemotaxis protein I, ... (4 entities in total) |
Functional Keywords | chemotaxis, signal transduction, membrane protein |
Biological source | Escherichia coli More |
Total number of polymer chains | 20 |
Total formula weight | 844126.60 |
Authors | Cassidy, C.K.,Qin, Z.,Zhang, P. (deposition date: 2023-01-10, release date: 2023-09-13, Last modification date: 2023-11-29) |
Primary citation | Cassidy, C.K.,Qin, Z.,Frosio, T.,Gosink, K.,Yang, Z.,Sansom, M.S.P.,Stansfeld, P.J.,Parkinson, J.S.,Zhang, P. Structure of the native chemotaxis core signaling unit from phage E-protein lysed E. coli cells. Mbio, 14:e0079323-e0079323, 2023 Cited by PubMed Abstract: Bacterial chemotaxis is a ubiquitous behavior that enables cell movement toward or away from specific chemicals. It serves as an important model for understanding cell sensory signal transduction and motility. Characterization of the molecular mechanisms underlying chemotaxis is of fundamental interest and requires a high-resolution structural picture of the sensing machinery, the chemosensory array. In this study, we combine cryo-electron tomography and molecular simulation to present the complete structure of the core signaling unit, the basic building block of chemosensory arrays, from . Our results provide new insight into previously poorly-resolved regions of the complex and offer a structural basis for designing new experiments to test mechanistic hypotheses. PubMed: 37772839DOI: 10.1128/mbio.00793-23 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (12 Å) |
Structure validation
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