132l

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132l, resolution 1.8Å

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STRUCTURAL CONSEQUENCES OF REDUCTIVE METHYLATION OF LYSINE RESIDUES IN HEN EGG WHITE LYSOZYME: AN X-RAY ANALYSIS AT 1.8 ANGSTROMS RESOLUTION

Overview

Chemical modification of proteins has been and continues to be an, important biochemical tool for the study of protein structure and, function. One such type of approach has been the reductive methylation of, lysine residues. In order to address the consequences of such methylation, on the crystallization and structural properties of a protein, the, three-dimensional structure of hen egg white lysozyme in which all lysine, residues have been alkylated has been determined and refined to a nominal, resolution of 1.8 A and a crystallographic R factor of 17.3%. Crystals, used in the investigation were grown from 1.5-1.8 M MgSO4 and 50 mM Tris, at pH 8.0 and belonged to the space group P2(1)2(1)2(1) with unit cell, dimensions of a = 30.6 A, b = 56.3 A, c = 73.2 A, and one molecule per, asymmetric unit. It was not possible to grow crystals of the modified, lysozyme under the conditions normally employed for the hen egg white, protein. Overall, the three-dimensional structures of the native lysozyme, and the modified protein are very similar with only two surface loops, differing to any significant extent. Specifically, the positions of the, alpha-carbons for these two forms of the protein, excluding the surface, loops, superimpose with a root-mean-square value of 0.40 A. The magnitude, of the structural changes observed between the modified an unmodified, forms of lysozyme is similar to that seen when an identical protein, structure is solved in two different crystalline lattices.(ABSTRACT, TRUNCATED AT 250 WORDS)

About this Structure

132L is a Single protein structure of sequence from [1] with DML as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

Structural consequences of reductive methylation of lysine residues in hen egg white lysozyme: an X-ray analysis at 1.8-A resolution., Rypniewski WR, Holden HM, Rayment I, Biochemistry. 1993 Sep 21;32(37):9851-8. PMID:8373783

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