6EXR
CHEMOTAXIS PROTEIN CHEY FROM Pyrococcus horikoshiI
Summary for 6EXR
| Entry DOI | 10.2210/pdb6exr/pdb |
| Descriptor | 120aa long hypothetical chemotaxis protein (CheY) (1 entity in total) |
| Functional Keywords | signal transduction protein, signaling protein |
| Biological source | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
| Total number of polymer chains | 6 |
| Total formula weight | 79144.18 |
| Authors | Paithankar, K.S.,Enderle, M.E.,Wirthensohn, D.,Grininger, M.,Oesterhelt, D. (deposition date: 2017-11-09, release date: 2018-12-12, Last modification date: 2024-01-17) |
| Primary citation | Paithankar, K.S.,Enderle, M.,Wirthensohn, D.C.,Miller, A.,Schlesner, M.,Pfeiffer, F.,Rittner, A.,Grininger, M.,Oesterhelt, D. Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation. Acta Crystallogr.,Sect.F, 75:576-585, 2019 Cited by PubMed Abstract: Archaea are motile by the rotation of the archaellum. The archaellum switches between clockwise and counterclockwise rotation, and movement along a chemical gradient is possible by modulation of the switching frequency. This modulation involves the response regulator CheY and the archaellum adaptor protein CheF. In this study, two new crystal forms and protein structures of CheY are reported. In both crystal forms, CheY is arranged in a domain-swapped conformation. CheF, the protein bridging the chemotaxis signal transduction system and the motility apparatus, was recombinantly expressed, purified and subjected to X-ray data collection. PubMed: 31475924DOI: 10.1107/S2053230X19010896 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.16 Å) |
Structure validation
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