This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Student Projects for UMass Chemistry 423 Spring 2016 by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439.
Asp Receptor Ligand-binding domain (1wat)
Bacteria use this protein to"smell"their environment (PDB entry 1wat)
The ligand binding domain of the aspartate receptor (Initial view) ) is a dimer of two 4-helix bundles that is shown here with the aspartate ligand bound.[1] In this rainbow representation the N and C termini are at the bottom of the structure; this is where the connections to the transmembrane helices have been truncated.
Binding Interactions
When the protein is colored according to sequence conservation , residues at the ligand site are the most conserved.
Interactions that stabilize ligand binding[2] include hydrogen bonding from Tyr149 and Gln152 backbone carbonyls and Thr154 sidechain OH to the ligand amino group and hydrogen bonding from the sidechain nitrogens of Arg64, Arg69, and Arg73 to the two ligand carboxyl groups.
↑Yeh JI, Biemann HP, Pandit J, Koshland DE, Kim SH. The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding. J Biol Chem. 1993 May 5;268(13):9787-92. PMID:8486661
↑Milburn MV, Prive GG, Milligan DL, Scott WG, Yeh J, Jancarik J, Koshland DE Jr, Kim SH. Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science. 1991 Nov 29;254(5036):1342-7. PMID:1660187