2z5c

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[[Image:2z5c.jpg|left|200px]]<br /><applet load="2z5c" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2z5c.jpg|left|200px]]
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caption="2z5c, resolution 2.90&Aring;" />
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'''Crystal Structure of a Novel Chaperone Complex for Yeast 20S Proteasome Assembly'''<br />
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{{Structure
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|PDB= 2z5c |SIZE=350|CAPTION= <scene name='initialview01'>2z5c</scene>, resolution 2.90&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1]
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|GENE=
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}}
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'''Crystal Structure of a Novel Chaperone Complex for Yeast 20S Proteasome Assembly'''
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==Overview==
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Eukaryotic 20S proteasomes are composed of two alpha-rings and two beta-rings, which form an alphabetabetaalpha stacked structure. Here we describe a proteasome-specific chaperone complex, designated Dmp1-Dmp2, in budding yeast. Dmp1-Dmp2 directly bound to the alpha5 subunit to facilitate alpha-ring formation. In Deltadmp1 cells, alpha-rings lacking alpha4 and decreased formation of 20S proteasomes were observed. Dmp1-Dmp2 interacted with proteasome precursors early during proteasome assembly and dissociated from the precursors before the formation of half-proteasomes. Notably, the crystallographic structures of Dmp1 and Dmp2 closely resemble that of PAC3-a mammalian proteasome-assembling chaperone; nonetheless, neither Dmp1 nor Dmp2 showed obvious sequence similarity to PAC3. The structure of the Dmp1-Dmp2-alpha5 complex reveals how this chaperone functions in proteasome assembly and why it dissociates from proteasome precursors before the beta-rings are assembled.
==About this Structure==
==About this Structure==
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2Z5C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z5C OCA].
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2Z5C is a [[Protein complex]] structure of sequences 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=2Z5C OCA].
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==Reference==
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Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes., Yashiroda H, Mizushima T, Okamoto K, Kameyama T, Hayashi H, Kishimoto T, Niwa S, Kasahara M, Kurimoto E, Sakata E, Takagi K, Suzuki A, Hirano Y, Murata S, Kato K, Yamane T, Tanaka K, Nat Struct Mol Biol. 2008 Mar;15(3):228-36. Epub 2008 Feb 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18278057 18278057]
[[Category: Proteasome endopeptidase complex]]
[[Category: Proteasome endopeptidase complex]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: s. cerevisiae]]
[[Category: s. cerevisiae]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:00:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:52:15 2008''

Revision as of 16:52, 20 March 2008

Image:2z5c.jpg


PDB ID 2z5c

Drag the structure with the mouse to rotate
, resolution 2.90Å
Activity: Proteasome endopeptidase complex, with EC number 3.4.25.1
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of a Novel Chaperone Complex for Yeast 20S Proteasome Assembly


Overview

Eukaryotic 20S proteasomes are composed of two alpha-rings and two beta-rings, which form an alphabetabetaalpha stacked structure. Here we describe a proteasome-specific chaperone complex, designated Dmp1-Dmp2, in budding yeast. Dmp1-Dmp2 directly bound to the alpha5 subunit to facilitate alpha-ring formation. In Deltadmp1 cells, alpha-rings lacking alpha4 and decreased formation of 20S proteasomes were observed. Dmp1-Dmp2 interacted with proteasome precursors early during proteasome assembly and dissociated from the precursors before the formation of half-proteasomes. Notably, the crystallographic structures of Dmp1 and Dmp2 closely resemble that of PAC3-a mammalian proteasome-assembling chaperone; nonetheless, neither Dmp1 nor Dmp2 showed obvious sequence similarity to PAC3. The structure of the Dmp1-Dmp2-alpha5 complex reveals how this chaperone functions in proteasome assembly and why it dissociates from proteasome precursors before the beta-rings are assembled.

About this Structure

2Z5C is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes., Yashiroda H, Mizushima T, Okamoto K, Kameyama T, Hayashi H, Kishimoto T, Niwa S, Kasahara M, Kurimoto E, Sakata E, Takagi K, Suzuki A, Hirano Y, Murata S, Kato K, Yamane T, Tanaka K, Nat Struct Mol Biol. 2008 Mar;15(3):228-36. Epub 2008 Feb 17. PMID:18278057

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