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1xwo
From Proteopedia
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(New page: 200px<br /><applet load="1xwo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xwo, resolution 2.8Å" /> '''crystal structrue of ...)
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Revision as of 04:16, 21 November 2007
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crystal structrue of goose delta crystallin
Overview
Delta-crystallin is a soluble structural protein in avian eye lenses that, confers special refractive properties. In the presence of GdmCl, (guanidinium chloride), tetrameric delta-crystallin undergoes dissociation, via a dimeric state to a monomeric molten globule intermediate state. The, latter are denatured at higher GdmCl concentrations in a multi-state, manner. In the present study, the X-ray structure of goose, delta-crystallin was determined to 2.8 A (1 A=0.1 nm). In this structure, the first 25 N-terminal residues interact with a hydrophobic cavity in a, neighbouring molecule, stabilizing the quaternary structure of this, protein. When these 25 residues were deleted this did not produce any, gross structural changes, as judged by CD analysis, but slightly altered, tryptophan fluorescence and ANS (8-anilino-1-naphthalenesulphonic acid), spectra. The dimeric form was significantly identified as judged by, sedimentation velocity and nondenaturing gradient gel electrophoresis., This mutant had increased sensitivity to temperature denaturation and, GdmCl concentrations of 0.3-1.0 M. This protein was destabilized about 3.3, kcal/mol (1 kcal=4.184 kJ) due to N-terminal truncation. After incubation, at 37 degrees C N-terminal truncated proteins were prone to aggregation, suggesting the presence of the unstable dimeric conformation. An important, role for the N-terminus in dimer assembly of goose delta-crystallin is, proposed.
About this Structure
1XWO is a Single protein structure of sequence from Anser anser anser. Active as Argininosuccinate lyase, with EC number 4.3.2.1 Full crystallographic information is available from OCA.
Reference
The effect of N-terminal truncation on double-dimer assembly of goose delta-crystallin., Lee HJ, Lai YH, Wu SY, Chen YH, Biochem J. 2005 Dec 15;392(Pt 3):545-54. PMID:16101585
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