1lys

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Revision as of 21:52, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1lys" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lys, resolution 1.72Å" /> '''X-RAY STRUCTURE OF A...)
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1lys, resolution 1.72Å

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X-RAY STRUCTURE OF A MONOCLINIC FORM OF HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT 313K. COMPARISON OF TWO INDEPENDENT MOLECULES

OverviewOverview

A monoclinic crystal of hen egg lysozyme (HEL, E.C. 3.2.1.17) was obtained, at 313 K from a 10%(w/v) NaCl solution at pH 7.6 containing 5%(v/v), 1-propanol. Cell dimensions were a = 27.23, b = 63.66, c = 59.12 A and, beta = 92.9 degrees, and the space group was P2(1). The unit cell contains, four molecules (V(m) = 1.79 A(3) Da(-1)). The structure was solved by the, isomorphous replacement method with anomalous scattering followed by phase, improvement by the solvent-flattening method. The refinement of the, structure was carried out by the simulated-annealing method. The, conventional R value was 0.187 for 18 260 reflections [|F(o)| > 3sigma(F)], in the resolution range 10-1.72 A. The r.m.s. deviations from the ideal, bond distances and angles were 0.015 A and 3.0 degrees, respectively. The, two molecules in the asymmetric unit are related by a translation of half, a lattice unit along the a and c axes. The r.m.s. difference of equivalent, C(alpha) atoms between the two molecules was 0.64 A and the largest, difference was 3.57 A for Gly71. A significant structural change was, observed in the regions of residues 45-50, 65-73 and 100-104. The residues, 45-50, which connect two beta-strands, are shifted parallel to the, beta-sheet plane between the two molecules. The residues 100-104 belong to, the substrate-binding site (subsite A) and the high flexibility of this, region may be responsible for the binding of the substrate and the release, of reaction products.

About this StructureAbout this Structure

1LYS 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.

ReferenceReference

X-ray structure of a monoclinic form of hen egg-white lysozyme crystallized at 313 K. Comparison of two independent molecules., Harata K, Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):250-7. PMID:15299435

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