1n4e
From Proteopedia
(New page: 200px<br /> <applet load="1n4e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n4e, resolution 2.5Å" /> '''Crystal Structure of...) |
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| - | [[Image:1n4e.gif|left|200px]]<br /> | + | [[Image:1n4e.gif|left|200px]]<br /><applet load="1n4e" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1n4e" size=" | + | |
caption="1n4e, resolution 2.5Å" /> | caption="1n4e, resolution 2.5Å" /> | ||
'''Crystal Structure of a DNA Decamer Containing a Thymine-dimer'''<br /> | '''Crystal Structure of a DNA Decamer Containing a Thymine-dimer'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Two distinct dimerization contacts in calsequestrin crystals suggested a | + | Two distinct dimerization contacts in calsequestrin crystals suggested a mechanism for Ca(2+) regulation resulting from the occurrence of coupled Ca(2+) binding and protein polymerization. Ca(2+)-induced formation of one contact was proposed to lead to dimerization followed by Ca(2+)-induced formation of the second contact to bring about polymerization (). To test this mechanism, we compared canine cardiac calsequestrin and four truncation mutants with regard to their folding properties, structures, and Ca(2+)-induced polymerization. The wild-type calsequestrin and truncation mutants exhibited similar K(+)-induced folding and end-point structures as indicated by intrinsic fluorescence and circular dichroism, respectively, whereas the polymerization tendencies of the wild-type calsequestrin differed markedly from the polymerization tendencies of the truncation mutants. Static laser light scattering and 3,3'-dithiobis sulfosuccinimidyl-propionate cross-linking indicated that wild-type protein exhibited an initial Ca(2+)-induced dimerization, followed by additional oligomerization as the Ca(2+) concentration was raised or as the K(+) concentration was lowered. None of the truncation mutants exhibited clear stepwise oligomerization that depended on increasing Ca(2+) concentration. Comparison of the three-dimensional structure of rabbit skeletal calsequestrin with a homology model of canine cardiac calsequestrin from the point of view of our coupled Ca(2+) binding and polymerization mechanism leads to a possible explanation for the 2-fold reduced Ca(2+) binding capacity of cardiac calsequestrin despite very similar overall net negative charge for the two proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1N4E is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. The following page contains interesting information on the relation of 1N4E with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb91_1.html Thymine Dimers]]. Full crystallographic information is available from [http:// | + | 1N4E is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. The following page contains interesting information on the relation of 1N4E with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb91_1.html Thymine Dimers]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ren, Y.]] | [[Category: Ren, Y.]] | ||
[[Category: Sinha, N.]] | [[Category: Sinha, N.]] | ||
| - | [[Category: Taylor, J | + | [[Category: Taylor, J S.]] |
[[Category: Zhang, K.]] | [[Category: Zhang, K.]] | ||
[[Category: dna decamer]] | [[Category: dna decamer]] | ||
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[[Category: uv-damaged dna]] | [[Category: uv-damaged dna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:07 2008'' |
Revision as of 12:02, 21 February 2008
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Crystal Structure of a DNA Decamer Containing a Thymine-dimer
Overview
Two distinct dimerization contacts in calsequestrin crystals suggested a mechanism for Ca(2+) regulation resulting from the occurrence of coupled Ca(2+) binding and protein polymerization. Ca(2+)-induced formation of one contact was proposed to lead to dimerization followed by Ca(2+)-induced formation of the second contact to bring about polymerization (). To test this mechanism, we compared canine cardiac calsequestrin and four truncation mutants with regard to their folding properties, structures, and Ca(2+)-induced polymerization. The wild-type calsequestrin and truncation mutants exhibited similar K(+)-induced folding and end-point structures as indicated by intrinsic fluorescence and circular dichroism, respectively, whereas the polymerization tendencies of the wild-type calsequestrin differed markedly from the polymerization tendencies of the truncation mutants. Static laser light scattering and 3,3'-dithiobis sulfosuccinimidyl-propionate cross-linking indicated that wild-type protein exhibited an initial Ca(2+)-induced dimerization, followed by additional oligomerization as the Ca(2+) concentration was raised or as the K(+) concentration was lowered. None of the truncation mutants exhibited clear stepwise oligomerization that depended on increasing Ca(2+) concentration. Comparison of the three-dimensional structure of rabbit skeletal calsequestrin with a homology model of canine cardiac calsequestrin from the point of view of our coupled Ca(2+) binding and polymerization mechanism leads to a possible explanation for the 2-fold reduced Ca(2+) binding capacity of cardiac calsequestrin despite very similar overall net negative charge for the two proteins.
About this Structure
1N4E is a Protein complex structure of sequences from [1]. The following page contains interesting information on the relation of 1N4E with [Thymine Dimers]. Full crystallographic information is available from OCA.
Reference
Polymerization of calsequestrin. Implications for Ca2+ regulation., Park H, Wu S, Dunker AK, Kang C, J Biol Chem. 2003 May 2;278(18):16176-82. Epub 2003 Feb 19. PMID:12594204
Page seeded by OCA on Thu Feb 21 14:02:07 2008
Categories: Protein complex | Thymine Dimers | Kang, C. | Nadji, S. | Park, H. | Ren, Y. | Sinha, N. | Taylor, J S. | Zhang, K. | Dna decamer | Thymine dimer | Uv-damaged dna
