1xao
From Proteopedia
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| - | [[Image:1xao.gif|left|200px]] | + | [[Image:1xao.gif|left|200px]] |
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| - | '''Hsp40-Ydj1 dimerization domain''' | + | {{Structure |
| + | |PDB= 1xao |SIZE=350|CAPTION= <scene name='initialview01'>1xao</scene>, resolution 2.07Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= MAS5, YDJ1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | }} | ||
| + | |||
| + | '''Hsp40-Ydj1 dimerization domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XAO is a [ | + | 1XAO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XAO OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40., Wu Y, Li J, Jin Z, Fu Z, Sha B, J Mol Biol. 2005 Mar 4;346(4):1005-11. Epub 2005 Jan 16. PMID:[http:// | + | The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40., Wu Y, Li J, Jin Z, Fu Z, Sha B, J Mol Biol. 2005 Mar 4;346(4):1005-11. Epub 2005 Jan 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15701512 15701512] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sha, B.]] | [[Category: Sha, B.]] | ||
[[Category: Wu, Y.]] | [[Category: Wu, Y.]] | ||
| - | [[Category: beta | + | [[Category: beta sheet]] |
| - | ''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 15:07:19 2008'' |
Revision as of 13:07, 20 March 2008
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| , resolution 2.07Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | MAS5, YDJ1 (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Hsp40-Ydj1 dimerization domain
Overview
The molecular chaperone Hsp40 functions as a dimer. The dimer formation is critical for Hsp40 molecular chaperone activity to facilitate Hsp70 to refold non-native polypeptides. We have determined the crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 that is responsible for Ydj1 dimerization by MAD method. The C-terminal fragment of Ydj1 comprises of the domain III of Ydj1 and the Ydj1 C-terminal dimerization motif. The crystal structure indicates that the dimerization motif of type I Hsp40 Ydj1 differs significantly from that of yeast type II Hsp40. The C terminus of type I Hsp40 Ydj1 from one monomer forms beta-strands with the domain III from the other monomer in the homo-dimer. The L372 from Ydj1 C terminus inserts its side-chain into a hydrophobic pocket on domain III. The modeled full-length Ydj1 dimer structure reveals that a large cleft is formed between the two monomers. The domain IIs of Ydj1 monomers that contain the zinc-finger motifs points directly against each other.
About this Structure
1XAO is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40., Wu Y, Li J, Jin Z, Fu Z, Sha B, J Mol Biol. 2005 Mar 4;346(4):1005-11. Epub 2005 Jan 16. PMID:15701512
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