4lym
From Proteopedia
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CRYSTAL STRUCTURE OF LOW HUMIDITY TETRAGONAL LYSOZYME AT 2.1-ANGSTROMS RESOLUTION. VARIABILITY IN HYDRATION SHELL AND ITS STRUCTURAL CONSEQUENCES
Overview
Tetragonal crystals of hen egg white lysozyme undergo a reversible, transformation, accompanied by loss of water, when the relative humidity, of the environment is reduced to about 90%. The structure of the low, humidity form has been analyzed, using x-ray data collected at 88%, relative humidity, in order to explore the variability in protein, hydration caused by a change in the amount of water surrounding the, protein molecule and the consequent conformational perturbations in the, molecule. The structure has been refined by the restrained least-squares, method to an R value of 0.162 for 6269 observed reflections in the, 10-2.1-A resolution shell. The refined structure provides interesting, examples for the variability in helical parameters, the role of, interactions involving side chains and water in the stabilization of, secondary structural features, and favorable specific hydration sites. The, protein molecule as a whole moves slightly in the low humidity form from, its position in the native crystals. The hydration shell tends to move, along with the protein. Significant changes, however, occur in the, hydration shell. These changes cause structural perturbations in the, enzyme molecule, which are most pronounced in regions involved in, substrate binding.
About this Structure
4LYM is a Single protein structure of sequence from Gallus gallus. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Crystal structure of low humidity tetragonal lysozyme at 2.1-A resolution. Variability in hydration shell and its structural consequences., Kodandapani R, Suresh CG, Vijayan M, J Biol Chem. 1990 Sep 25;265(27):16126-31. PMID:2398048
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