1fpo: Difference between revisions
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'''HSC20 (HSCB), A J-TYPE CO-CHAPERONE FROM E. COLI''' | {{Structure | ||
|PDB= 1fpo |SIZE=350|CAPTION= <scene name='initialview01'>1fpo</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''HSC20 (HSCB), A J-TYPE CO-CHAPERONE FROM E. COLI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FPO is a [ | 1FPO is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11124030 11124030] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: molecular chaperone]] | [[Category: molecular chaperone]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:12:20 2008'' | ||
Revision as of 09:12, 20 March 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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