1ud0
From Proteopedia
(New page: 200px<br /><applet load="1ud0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ud0, resolution 3.45Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1ud0.gif|left|200px]]<br /><applet load="1ud0" size=" | + | [[Image:1ud0.gif|left|200px]]<br /><applet load="1ud0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ud0, resolution 3.45Å" /> | caption="1ud0, resolution 3.45Å" /> | ||
'''CRYSTAL STRUCTURE OF THE C-TERMINAL 10-kDA SUBDOMAIN OF HSC70'''<br /> | '''CRYSTAL STRUCTURE OF THE C-TERMINAL 10-kDA SUBDOMAIN OF HSC70'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 70-kDa heat shock proteins (Hsp70), including the cognates (Hsc70), are molecular chaperones that prevent misfolding and aggregation of | + | The 70-kDa heat shock proteins (Hsp70), including the cognates (Hsc70), are molecular chaperones that prevent misfolding and aggregation of polypeptides in cells under both normal and stressed conditions. They are composed of two major structural domains: an N-terminal 44-kDa ATPase domain and a C-terminal 30-kDa substrate binding domain. The 30-kDa domain can be divided into an 18-kDa subdomain and a 10-kDa subdomain. Here we report the crystal structure of the 10-kDa subdomain of rat Hsc70 at 3.45 A. Its helical region adopted a helix-loop-helix fold. This conformation is different from the equivalent subdomain of DnaK, the bacterial homologue of Hsc70. Moreover, in the crystalline state, the 10-kDa subdomain formed dimers. The results of gel filtration chromatography further supported the view that this subdomain was self-associated. Upon gel filtration, Hsc70 was found to exist as a mixture of monomers, dimers, and oligomers, but the 60-kDa fragment was predominantly found to exist as monomers. These findings suggest that the alpha-helical region of the 10-kDa subdomain dictates the chaperone self-association. |
==About this Structure== | ==About this Structure== | ||
| - | 1UD0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1UD0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UD0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chou, C | + | [[Category: Chou, C C.]] |
[[Category: Forouhar, F.]] | [[Category: Forouhar, F.]] | ||
| - | [[Category: Hsiao, C | + | [[Category: Hsiao, C D.]] |
[[Category: Wang, C.]] | [[Category: Wang, C.]] | ||
| - | [[Category: Yeh, Y | + | [[Category: Yeh, Y H.]] |
[[Category: NA]] | [[Category: NA]] | ||
[[Category: hsc70]] | [[Category: hsc70]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:07 2008'' |
Revision as of 13:23, 21 February 2008
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CRYSTAL STRUCTURE OF THE C-TERMINAL 10-kDA SUBDOMAIN OF HSC70
Overview
The 70-kDa heat shock proteins (Hsp70), including the cognates (Hsc70), are molecular chaperones that prevent misfolding and aggregation of polypeptides in cells under both normal and stressed conditions. They are composed of two major structural domains: an N-terminal 44-kDa ATPase domain and a C-terminal 30-kDa substrate binding domain. The 30-kDa domain can be divided into an 18-kDa subdomain and a 10-kDa subdomain. Here we report the crystal structure of the 10-kDa subdomain of rat Hsc70 at 3.45 A. Its helical region adopted a helix-loop-helix fold. This conformation is different from the equivalent subdomain of DnaK, the bacterial homologue of Hsc70. Moreover, in the crystalline state, the 10-kDa subdomain formed dimers. The results of gel filtration chromatography further supported the view that this subdomain was self-associated. Upon gel filtration, Hsc70 was found to exist as a mixture of monomers, dimers, and oligomers, but the 60-kDa fragment was predominantly found to exist as monomers. These findings suggest that the alpha-helical region of the 10-kDa subdomain dictates the chaperone self-association.
About this Structure
1UD0 is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the C-terminal 10-kDa subdomain of Hsc70., Chou CC, Forouhar F, Yeh YH, Shr HL, Wang C, Hsiao CD, J Biol Chem. 2003 Aug 8;278(32):30311-6. Epub 2003 May 28. PMID:12773536
Page seeded by OCA on Thu Feb 21 15:23:07 2008
Categories: Rattus norvegicus | Single protein | Chou, C C. | Forouhar, F. | Hsiao, C D. | Wang, C. | Yeh, Y H. | NA | Hsc70
