2A0B
HISTIDINE-CONTAINING PHOSPHOTRANSFER DOMAIN OF ARCB FROM ESCHERICHIA COLI
Summary for 2A0B
Entry DOI | 10.2210/pdb2a0b/pdb |
Descriptor | HPT DOMAIN, ZINC ION (3 entities in total) |
Functional Keywords | sensory transduction, histidine kinase, phosphotransfer, two-component system, four-helix bundle |
Biological source | Escherichia coli |
Cellular location | Cell inner membrane; Multi-pass membrane protein: P22763 |
Total number of polymer chains | 1 |
Total formula weight | 14079.35 |
Authors | Kato, M.,Mizuno, T.,Shimizu, T.,Hakoshima, T. (deposition date: 1998-04-02, release date: 1998-06-17, Last modification date: 2024-02-14) |
Primary citation | Kato, M.,Mizuno, T.,Shimizu, T.,Hakoshima, T. Refined structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57 A resolution. Acta Crystallogr.,Sect.D, 55:1842-1849, 1999 Cited by PubMed Abstract: The crystal structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli has been refined to 1.57 A resolution, using the coordinates of the earlier 2.06 A structure as a starting model. The final model contained 956 protein atoms, one zinc ion and 156 water molecules, with an R factor of 19.0%. The high-resolution electron-density maps clearly revealed additional solvent molecules and seven discrete rotamers in the protein side chains. One residue, Met755, was fully buried but was able to occupy the space in the hydrophobic core by means of the two-state conformation of its side chain. One water molecule was buried in the protein core and contributed to the rigidity of the HPt domain, cooperating in the coordination of the zinc ion. PubMed: 10531481DOI: 10.1107/S0907444999010392 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
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