135l

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(New page: 200px<br /><applet load="135l" size="450" color="white" frame="true" align="right" spinBox="true" caption="135l, resolution 1.30&Aring;" /> '''X-RAY STRUCTURE OF M...)
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Revision as of 08:19, 20 November 2007


135l, resolution 1.30Å

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X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION

Overview

Monoclinic crystals of turkey egg lysozyme (TEL, E.C. 3.2.1.17) were, obtained from 2.2 M ammonium sulfate solution at pH 4.2. They belong to, space group P2(1) with unit-cell dimensions a = 38.07, b = 33.20, c =, 46.12 A and beta = 110.1 degrees, and contain one molecule in the, asymmetric unit (V(m) = 1.91 A(3) Da(-1)). The three-dimensional structure, of TEL was solved by the method of multiple isomorphous replacement with, anomalous scattering. Area detector data to 1.5 A resolution from native, and heavy-atom derivatives were used for the structure determination. The, structure was refined by the simulated-annealing method with diffraction, data of 10-1.30 A resolution. The conventional R factor was 0.189. The, root-mean-square deviations from ideal bond distances and angles were, 0.016 A and 2.9 degrees, respectively. The backbone structure of TEL is, very similar to that of hen egg lysozyme (HEL) and the difference in seven, amino-acid residues does not affect the basic folding of the polypeptide, chain. Except for the region from Gly101 to Gly104, the geometry of the, active-site cleft is conserved between TEL and HEL. The Gly101 residue is, located at the end of the sugar-binding site and the structural change in, this region between TEL and HEL is considered to be responsible for the, difference in their enzymatic properties.

About this Structure

135L is a Single protein structure of sequence from [1]. This structure superseeds the now removed PDB entry 1LZ3. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution., Harata K, Acta Crystallogr D Biol Crystallogr. 1993 Sep 1;49(Pt 5):497-504. PMID:15299509

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