1lys
From Proteopedia
(New page: 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...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1lys.jpg|left|200px]]<br /><applet load="1lys" size=" | + | [[Image:1lys.jpg|left|200px]]<br /><applet load="1lys" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lys, resolution 1.72Å" /> | caption="1lys, resolution 1.72Å" /> | ||
'''X-RAY STRUCTURE OF A MONOCLINIC FORM OF HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT 313K. COMPARISON OF TWO INDEPENDENT MOLECULES'''<br /> | '''X-RAY STRUCTURE OF A MONOCLINIC FORM OF HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT 313K. COMPARISON OF TWO INDEPENDENT MOLECULES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A monoclinic crystal of hen egg lysozyme (HEL, E.C. 3.2.1.17) was obtained | + | 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 Structure== | ==About this Structure== | ||
| - | 1LYS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http:// | + | 1LYS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LYS OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 17: | ||
[[Category: hydrolase(o-glycosyl)]] | [[Category: hydrolase(o-glycosyl)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:41 2008'' |
Revision as of 11:49, 21 February 2008
|
X-RAY STRUCTURE OF A MONOCLINIC FORM OF HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT 313K. COMPARISON OF TWO INDEPENDENT MOLECULES
Overview
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 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.
Reference
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
Page seeded by OCA on Thu Feb 21 13:49:41 2008
