 |
|
Title
|
|
Analysis of an enzyme-substrate complex by X-ray crystallography and transferred nuclear Overhauser enhancement measurements: porcine pancreatic elastase and a hexapeptide.
|
|
|
Authors
|
|
E.F.Meyer,
G.M.Clore,
A.M.Gronenborn,
H.A.Hansen.
|
|
|
Ref.
|
|
Biochemistry, 1988,
27,
725-730.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The hexapeptide substrate Thr-Pro-nVal-NMeLeu-Tyr-Thr reacts with porcine
pancreatic elastase sufficiently slowly that accelerated crystallographic data
collection procedures and two-dimensional transferred nuclear Overhauser
enhancement measurements could be used to study the geometry of binding. Both
studies report a time-averaged population of the Michaelis complex state, prior
to proteolysis. This result provides an important data point along the reaction
coordinate pathway for serine proteases. Crystallographic data to 1.80-A
resolution were used in the structure analysis with refinement to an R-factor of
0.19.
|
|
|
|