Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium
| Autor: | Daniel L. Milligan, Daniel E. Koshland, Sung-Hou Kim, Jarmila Jancarik, William G. Scott |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Salmonella typhimurium
Biochemistry & Molecular Biology endocrine system diseases Receptors Cell Surface TRANSMEMBRANE Ligands Microbiology Serine Vaccine Related Medicinal and Biomolecular Chemistry X-Ray Diffraction Structural Biology Cell surface receptor Biodefense Receptors Receptors Amino Acid ASPARTATE Binding site Receptor Molecular Biology Aspartic Acid biology RECEPTOR Chemotaxis Prevention nutritional and metabolic diseases Periplasmic space biology.organism_classification Enterobacteriaceae Aspartate carbamoyltransferase Amino Acid Infectious Diseases Emerging Infectious Diseases Biochemistry Cell Surface LIGAND-BINDING Biochemistry and Cell Biology Crystallization Digestive Diseases hormones hormone substitutes and hormone antagonists |
| Zdroj: | Journal of molecular biology, vol 221, iss 1 Jancarik, J; Scott, WG; Milligan, DL; Koshland, DE; & Kim, SH. (1991). Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium. Journal of Molecular Biology, 221(1), 31-34. doi: 10.1016/0022-2836(91)80198-4. UC Santa Cruz: Retrieved from: http://www.escholarship.org/uc/item/8br6883h |
| Popis: | The periplasmic domain of the aspartate chemotaxis receptor from Salmonella typhimurium has been crystallized in the presence and absence of bound aspartate. Both crystal forms were grown by precipitation with lithium sulfate and diffract to 1·8 Å resolution. The aspartate receptor structure is believed to be prototypical of a large class of receptors including those for polypeptide growth factor hormones as well as those for small chemotaxis-affector molecules such as aspartate and serine. © 1991. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|