Extraction of functional motion in trypsin crystal structures.
The analysis of anisotropic atomic displacement parameters for the direct extraction of functionally relevant motion from X-ray crystal structures of Fusarium oxysporum trypsin is presented. Several atomic resolution structures complexed with inhibitors or substrates and determined at different pH values and temperatures were investigated. The analysis revealed a breathing-like molecular motion conserved across trypsin structures from two organisms and three different crystal forms. Directional motion was observed suggesting a change of the width of the substrate-binding cleft and a change in the length of the specificity pocket. The differences in direction of motion across the structures are dependent on the mode of substrate or inhibitor binding and the chemical environment around the active-site residues. Together with the occurrence of multiple-residue conformers, they reflect spatial rearrangement throughout the deacylation pathway.
Schmidt
Andrea
A
European Molecular Biology Laboratory (EMBL), Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany. andrea@embl-hamburg.de
Lamzin
Victor S
VS
D016880:Anisotropy; D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray / Q000379:methods*; D005670:Fusarium / Q000201:enzymology; D008958:Models, Molecular; D009038:Motion; D011487:Protein Conformation; D014357:Trypsin / Q000737:chemistry*
D014357:Trypsin