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1t7s

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(New page: 200px<br /><applet load="1t7s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t7s, resolution 2.80&Aring;" /> '''Structural Genomics ...)
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[[Image:1t7s.gif|left|200px]]<br /><applet load="1t7s" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1t7s.gif|left|200px]]<br /><applet load="1t7s" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1t7s, resolution 2.80&Aring;" />
caption="1t7s, resolution 2.80&Aring;" />
'''Structural Genomics of Caenorhabditis elegans: Structure of BAG-1 protein'''<br />
'''Structural Genomics of Caenorhabditis elegans: Structure of BAG-1 protein'''<br />
==Overview==
==Overview==
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Binding of the BAG domain to the eukaryotic chaperone heat-shock protein, (Hsp70) promotes ATP-dependent release of the protein substrate from, Hsp70. Although the murine and human BAG domains have been shown to form, an antiparallel three-helix bundle, the Caenorhabditis elegans BAG domain, is formed by two antiparallel helices, while the third helix is extended, away and stabilized by crystal-packing interactions. A small beta-sheet, between helices 2 and 3 interferes with formation of the intramolecular, three-helix bundle. However, intermolecular three-helix bundles are, observed throughout the crystal packing and suggest that stable functional, dimers and tetramers can be formed in solution. The structure may, represent a new folding type of the BAG domain.
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Binding of the BAG domain to the eukaryotic chaperone heat-shock protein (Hsp70) promotes ATP-dependent release of the protein substrate from Hsp70. Although the murine and human BAG domains have been shown to form an antiparallel three-helix bundle, the Caenorhabditis elegans BAG domain is formed by two antiparallel helices, while the third helix is extended away and stabilized by crystal-packing interactions. A small beta-sheet between helices 2 and 3 interferes with formation of the intramolecular three-helix bundle. However, intermolecular three-helix bundles are observed throughout the crystal packing and suggest that stable functional dimers and tetramers can be formed in solution. The structure may represent a new folding type of the BAG domain.
==About this Structure==
==About this Structure==
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1T7S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T7S OCA].
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1T7S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7S OCA].
==Reference==
==Reference==
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[[Category: Bunzel, R.]]
[[Category: Bunzel, R.]]
[[Category: Li, S.]]
[[Category: Li, S.]]
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[[Category: Luan, C.H.]]
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[[Category: Luan, C H.]]
[[Category: Luo, M.]]
[[Category: Luo, M.]]
[[Category: Pruett, P.]]
[[Category: Pruett, P.]]
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[[Category: SECSG, Southeast.Collaboratory.for.Structural.Genomics.]]
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[[Category: SECSG, Southeast Collaboratory for Structural Genomics.]]
[[Category: Schormann, N.]]
[[Category: Schormann, N.]]
[[Category: Symersky, J.]]
[[Category: Symersky, J.]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:03:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:48 2008''

Revision as of 13:10, 21 February 2008


1t7s, resolution 2.80Å

Drag the structure with the mouse to rotate

Structural Genomics of Caenorhabditis elegans: Structure of BAG-1 protein

Overview

Binding of the BAG domain to the eukaryotic chaperone heat-shock protein (Hsp70) promotes ATP-dependent release of the protein substrate from Hsp70. Although the murine and human BAG domains have been shown to form an antiparallel three-helix bundle, the Caenorhabditis elegans BAG domain is formed by two antiparallel helices, while the third helix is extended away and stabilized by crystal-packing interactions. A small beta-sheet between helices 2 and 3 interferes with formation of the intramolecular three-helix bundle. However, intermolecular three-helix bundles are observed throughout the crystal packing and suggest that stable functional dimers and tetramers can be formed in solution. The structure may represent a new folding type of the BAG domain.

About this Structure

1T7S is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.

Reference

Structural genomics of Caenorhabditis elegans: structure of the BAG domain., Symersky J, Zhang Y, Schormann N, Li S, Bunzel R, Pruett P, Luan CH, Luo M, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1606-10. Epub 2004, Aug 26. PMID:15333932

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