2z5e: Difference between revisions

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[[Image:2z5e.~~jpg~~|left|200px]]

[[Image:2z5e.png|left|200px]]

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~~'''~~Crystal Structure of Proteasome Assembling Chaperone 3~~'''~~

===Crystal Structure of Proteasome Assembling Chaperone 3===

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_18278057}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18278057 is the PubMed ID number.

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==About this Structure==

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[[Category: Homodimer]]

[[Category: Proteasome]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 19~~:57:56 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:08:55 2008''

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-[[Image:2z5e.jpg|left|200px]]
+{{Seed}}
+[[Image:2z5e.png|left|200px]]
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 {{STRUCTURE_2z5e|  PDB=2z5e  |  SCENE=  }}
-'''Crystal Structure of Proteasome Assembling Chaperone 3'''
+===Crystal Structure of Proteasome Assembling Chaperone 3===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18278057}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18278057 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18278057}}
 ==About this Structure==
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 [[Category: Homodimer]]
 [[Category: Proteasome]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 19:57:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:08:55 2008''