Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium.
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 A 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.
Jancarik
J
J
Department of Chemistry, University of California, Berkeley 94720.
Scott
W G
WG
Milligan
D L
DL
Koshland
D E
DE
Kim
S H
SH
D001224:Aspartic Acid / Q000378:metabolism*; D002633:Chemotaxis; D003460:Crystallization; D008024:Ligands; D017459:Receptors, Amino Acid; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism; D012486:Salmonella typhimurium / Q000378:metabolism*; D014961:X-Ray Diffraction
D008024:Ligands; D017459:Receptors, Amino Acid; D011956:Receptors, Cell Surface; C031959:aspartic acid receptor; D001224:Aspartic Acid