1tec
|
CRYSTALLOGRAPHIC REFINEMENT BY INCORPORATION OF MOLECULAR DYNAMICS. THE THERMOSTABLE SERINE PROTEASE THERMITASE COMPLEXED WITH EGLIN-C
OverviewOverview
In order to investigate the principles of protein thermostability, the, crystal structure of thermitase from Thermoactinomyces vulgaris, a, thermostable member of the subtilisin family of serine proteases, has been, determined in a complex with eglin c. Eglin c is a serine protease, inhibitor from the leech Hirudo medicinalis. After data collection with a, television area-detector diffractometer and initial structure solution by, molecular-replacement methods, crystallographic refinement proceeded with, incorporation of molecular-dynamics techniques. It appeared that this, refinement procedure has a large convergence radius with movements of more, than 5 A for many atoms. Two procedures for the crystallographic, molecular-dynamics refinement have been tested. They differed mainly in, time span and weight on the X-ray 'energy'. The best results were obtained, with a procedure which allowed the molecular-dynamics technique to search, a large area in conformational space by having less weight on the X-ray, restraints and allowing more time. The use of molecular-dynamics, refinement considerably simplified the laborious and difficult task of, fitting the model in its electron density during the refinement process., The final crystallographic R factor is 17.9% at 2.2 A resolution.
About this StructureAbout this Structure
1TEC is a Protein complex structure of sequences from Hirudo medicinalis and Thermoactinomyces vulgaris with CA and NA as ligands. Active as Thermitase, with EC number 3.4.21.66 Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic refinement by incorporation of molecular dynamics: thermostable serine protease thermitase complexed with eglin c., Gros P, Fujinaga M, Dijkstra BW, Kalk KH, Hol WG, Acta Crystallogr B. 1989 Oct 1;45 ( Pt 5):488-99. PMID:2688688
Page seeded by OCA on Wed Nov 21 03:11:55 2007