1xvm

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1xvm, resolution 1.10Å

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Trypsin from Fusarium oxysporum- room temperature to atomic resolution

Overview

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.

About this Structure

1XVM is a Single protein structure of sequence from Fusarium oxysporum. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.

Reference

Extraction of functional motion in trypsin crystal structures., Schmidt A, Lamzin VS, Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1132-9. Epub 2005, Jul 20. PMID:16041079

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