1fpo
From Proteopedia
(New page: 200px<br /><applet load="1fpo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fpo, resolution 1.80Å" /> '''HSC20 (HSCB), A J-TY...) |
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| - | [[Image:1fpo.jpg|left|200px]]<br /><applet load="1fpo" size=" | + | [[Image:1fpo.jpg|left|200px]]<br /><applet load="1fpo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fpo, resolution 1.80Å" /> | caption="1fpo, resolution 1.80Å" /> | ||
'''HSC20 (HSCB), A J-TYPE CO-CHAPERONE FROM E. COLI'''<br /> | '''HSC20 (HSCB), A J-TYPE CO-CHAPERONE FROM E. COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Hsc20 is a 20 kDa J-protein that regulates the ATPase activity and | + | Hsc20 is a 20 kDa J-protein that regulates the ATPase activity and peptide-binding specificity of Hsc66, an hsp70-class molecular chaperone. We report herein the crystal structure of Hsc20 from Escherichia coli determined to a resolution of 1.8 A using a combination of single isomorphous replacement (SIR) and multi-wavelength anomalous diffraction (MAD). The overall structure of Hsc20 consists of two distinct domains, an N-terminal J-domain containing residues 1-75 connected by a short loop to a C-terminal domain containing residues 84-171. The structure of the J-domain, involved in interactions with Hsc66, resembles the alpha-topology of J-domain fragments of Escherichia coli DnaJ and human Hdj1 previously determined by solution NMR methods. The C-terminal domain, implicated in binding and targeting proteins to Hsc66, consists of a three-helix bundle in which two helices comprise an anti-parallel coiled-coil. The two domains make contact through an extensive hydrophobic interface ( approximately 650 A(2)) suggesting that their relative orientations are fixed. Thus, Hsc20, in addition to its role in the regulation of the ATPase activity of Hsc66, may also function as a rigid scaffold to facilitate positioning of the protein substrates targeted to Hsc66. |
==About this Structure== | ==About this Structure== | ||
| - | 1FPO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1FPO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cupp-Vickery, J | + | [[Category: Cupp-Vickery, J R.]] |
| - | [[Category: Vickery, L | + | [[Category: Vickery, L E.]] |
[[Category: molecular chaperone]] | [[Category: molecular chaperone]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:14 2008'' |
Revision as of 10:41, 21 February 2008
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HSC20 (HSCB), A J-TYPE CO-CHAPERONE FROM E. COLI
Overview
Hsc20 is a 20 kDa J-protein that regulates the ATPase activity and peptide-binding specificity of Hsc66, an hsp70-class molecular chaperone. We report herein the crystal structure of Hsc20 from Escherichia coli determined to a resolution of 1.8 A using a combination of single isomorphous replacement (SIR) and multi-wavelength anomalous diffraction (MAD). The overall structure of Hsc20 consists of two distinct domains, an N-terminal J-domain containing residues 1-75 connected by a short loop to a C-terminal domain containing residues 84-171. The structure of the J-domain, involved in interactions with Hsc66, resembles the alpha-topology of J-domain fragments of Escherichia coli DnaJ and human Hdj1 previously determined by solution NMR methods. The C-terminal domain, implicated in binding and targeting proteins to Hsc66, consists of a three-helix bundle in which two helices comprise an anti-parallel coiled-coil. The two domains make contact through an extensive hydrophobic interface ( approximately 650 A(2)) suggesting that their relative orientations are fixed. Thus, Hsc20, in addition to its role in the regulation of the ATPase activity of Hsc66, may also function as a rigid scaffold to facilitate positioning of the protein substrates targeted to Hsc66.
About this Structure
1FPO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli., Cupp-Vickery JR, Vickery LE, J Mol Biol. 2000 Dec 15;304(5):835-45. PMID:11124030
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