The periplasmic leucine-binding protein is the primary receptor for the leucine transport system in Escherichia coli. We report here the structure of an open ligand-free form solved by molecular replacement and refined at 1.5-Å resolution.
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The genes encoding the leucine binding proteins in E coli have been cloned and their DNA sequences have been determined. One of the binding proteins ...
We observed leucine binding to all proteins. LS binds L-phenylalanine but the mutation from Trp to Tyr or Phe disallows this ligand and expands the binding ...
The L-leucine-binding protein structure is, as expected, very similar to the Leu/Ile/Val-binding protein structure; both are in the unliganded conformation with ...
Sep 29, 2017 · SPR analysis indicated that BC-LI-0186 does not bind to Sestrin2, another leucine-binding protein (Supplementary Fig. 1g). These results ...
Fully understanding how leucine binding causes dissociation of Sestrin2 from GATOR2 will probably require ascertaining the structure of either apo-Sestrin2 or ...
This domain is found in periplasmic binding proteins, mainly belonging to the leucine-binding and Leu/Ile/Val-binding proteins.
Sep 9, 2013 · Here, we report a mechanical unfolding study of a 346-residue, two-domain leucine binding protein (LBP) from the bacterial periplasm. Forced ...