1hsx

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[[Image:1hsx.gif|left|200px]]
[[Image:1hsx.gif|left|200px]]
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{{Structure
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|PDB= 1hsx |SIZE=350|CAPTION= <scene name='initialview01'>1hsx</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1hsx", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1hsx| PDB=1hsx | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hsx OCA], [http://www.ebi.ac.uk/pdbsum/1hsx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hsx RCSB]</span>
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'''LYSOZYME GROWN AT BASIC PH AND ITS LOW HUMIDITY VARIANT'''
'''LYSOZYME GROWN AT BASIC PH AND ITS LOW HUMIDITY VARIANT'''
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[[Category: Sukumar, N.]]
[[Category: Sukumar, N.]]
[[Category: Vijayan, M.]]
[[Category: Vijayan, M.]]
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[[Category: enzyme-orthorhombic form]]
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[[Category: Enzyme-orthorhombic form]]
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[[Category: glycosidase]]
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[[Category: Glycosidase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:11:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:09:57 2008''
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Revision as of 16:11, 2 May 2008

Template:STRUCTURE 1hsx

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. 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 Page seeded by OCA on Fri May 2 19:11:50 2008

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