1DJM
SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI
Summary for 1DJM
| Entry DOI | 10.2210/pdb1djm/pdb |
| Descriptor | CHEMOTAXIS PROTEIN Y (1 entity in total) |
| Functional Keywords | befx, chey, response regulator, chemotaxis, two-component, signaling protein |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm: P06143 |
| Total number of polymer chains | 1 |
| Total formula weight | 14112.33 |
| Authors | Cho, H.S.,Lee, S.Y.,Yan, D.,Pan, X.,Parkinson, J.S.,Kustu, S.,Wemmer, D.E.,Pelton, J.G. (deposition date: 1999-12-03, release date: 2000-04-05, Last modification date: 2024-05-22) |
| Primary citation | Cho, H.S.,Lee, S.Y.,Yan, D.,Pan, X.,Parkinson, J.S.,Kustu, S.,Wemmer, D.E.,Pelton, J.G. NMR structure of activated CheY. J.Mol.Biol., 297:543-551, 2000 Cited by PubMed Abstract: The CheY protein is the response regulator in bacterial chemotaxis. Phosphorylation of a conserved aspartyl residue induces structural changes that convert the protein from an inactive to an active state. The short half-life of the aspartyl-phosphate has precluded detailed structural analysis of the active protein. Persistent activation of Escherichia coli CheY was achieved by complexation with beryllofluoride (BeF(3)(-)) and the structure determined by NMR spectroscopy to a backbone r.m.s.d. of 0.58(+/-0.08) A. Formation of a hydrogen bond between the Thr87 OH group and an active site acceptor, presumably Asp57.BeF(3)(-), stabilizes a coupled rearrangement of highly conserved residues, Thr87 and Tyr106, along with displacement of beta4 and H4, to yield the active state. The coupled rearrangement may be a more general mechanism for activation of receiver domains. PubMed: 10731410DOI: 10.1006/jmbi.2000.3595 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
