1hsx
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(New page: 200px<br /><applet load="1hsx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hsx, resolution 1.90Å" /> '''LYSOZYME GROWN AT BA...)
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Revision as of 14:41, 20 November 2007
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LYSOZYME GROWN AT BASIC PH AND ITS LOW HUMIDITY VARIANT
Overview
The structures of orthorhombic lysozyme grown at basic pH and its, low-humidity variant have been solved and refined at 1.9 and 2.0 A, resolution, respectively. A comparison of the native structure with those, of crystals grown at acidic pH does not show any systematic pH-dependent, difference in the molecular geometry. The conformations, mutual, orientation and interactions of the catalytic residues Glu35 and Asp52, also remain unchanged. However, comparison between the native and, low-humidity forms in the orthorhombic form show that the changes in, molecular geometry which accompany the water-mediated transformation to, the low-humidity form are more pronounced in the C-terminal residues than, in the other regions of the molecule. During the transformation from the, native to the low-humidity form, the locations of only about half the, water molecules in the hydration shell remain unchanged, but the hydration, shell as a whole moves along with the protein molecule.
About this Structure
1HSX 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
Structures of orthorhombic lysozyme grown at basic pH and its low-humidity variant., Sukumar N, Biswal BK, Vijayan M, Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):934-7. PMID:10089340
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