1hsx
From Proteopedia
(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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| - | [[Image:1hsx.gif|left|200px]]<br /><applet load="1hsx" size=" | + | [[Image:1hsx.gif|left|200px]]<br /><applet load="1hsx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hsx, resolution 1.90Å" /> | caption="1hsx, resolution 1.90Å" /> | ||
'''LYSOZYME GROWN AT BASIC PH AND ITS LOW HUMIDITY VARIANT'''<br /> | '''LYSOZYME GROWN AT BASIC PH AND ITS LOW HUMIDITY VARIANT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structures of orthorhombic lysozyme grown at basic pH and its | + | 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== | ==About this Structure== | ||
| - | 1HSX 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:// | + | 1HSX 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=1HSX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Biswal, B | + | [[Category: Biswal, B K.]] |
[[Category: Sukumar, N.]] | [[Category: Sukumar, N.]] | ||
[[Category: Vijayan, M.]] | [[Category: Vijayan, M.]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:32 2008'' |
Revision as of 11:04, 21 February 2008
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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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