1yuw
From Proteopedia
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| - | [[Image:1yuw.gif|left|200px]] | + | [[Image:1yuw.gif|left|200px]] |
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| - | '''crystal structure of bovine hsc70(aa1-554)E213A/D214A mutant''' | + | {{Structure |
| + | |PDB= 1yuw |SIZE=350|CAPTION= <scene name='initialview01'>1yuw</scene>, resolution 2.600Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= HSPA8, HSC70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | ||
| + | }} | ||
| + | |||
| + | '''crystal structure of bovine hsc70(aa1-554)E213A/D214A mutant''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YUW is a [ | + | 1YUW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUW OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis of interdomain communication in the Hsc70 chaperone., Jiang J, Prasad K, Lafer EM, Sousa R, Mol Cell. 2005 Nov 23;20(4):513-24. PMID:[http:// | + | Structural basis of interdomain communication in the Hsc70 chaperone., Jiang J, Prasad K, Lafer EM, Sousa R, Mol Cell. 2005 Nov 23;20(4):513-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16307916 16307916] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: chaperone]] | [[Category: 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 15:27:48 2008'' |
Revision as of 13:27, 20 March 2008
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| , resolution 2.600Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | HSPA8, HSC70 (Bos taurus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
crystal structure of bovine hsc70(aa1-554)E213A/D214A mutant
Overview
Hsp70 family proteins are highly conserved chaperones involved in protein folding, degradation, targeting and translocation, and protein complex remodeling. They are comprised of an N-terminal nucleotide binding domain (NBD) and a C-terminal protein substrate binding domain (SBD). ATP binding to the NBD alters SBD conformation and substrate binding kinetics, but an understanding of the mechanism of interdomain communication has been hampered by the lack of a crystal structure of an intact chaperone. We report here the 2.6 angstroms structure of a functionally intact bovine Hsc70 (bHsc70) and a mutational analysis of the observed interdomain interface and the immediately adjacent interdomain linker. This analysis identifies interdomain interactions critical for chaperone function and supports an allosteric mechanism in which the interdomain linker invades and disrupts the interdomain interface when ATP binds.
About this Structure
1YUW is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structural basis of interdomain communication in the Hsc70 chaperone., Jiang J, Prasad K, Lafer EM, Sousa R, Mol Cell. 2005 Nov 23;20(4):513-24. PMID:16307916
Page seeded by OCA on Thu Mar 20 15:27:48 2008
