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| {{STRUCTURE_3cf0| PDB=3cf0 | SCENE= }} | | {{STRUCTURE_3cf0| PDB=3cf0 | SCENE= }} |
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| '''Structure of D2 subdomain of P97/VCP in complex with ADP'''
| | ===Structure of D2 subdomain of P97/VCP in complex with ADP=== |
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| ==Overview==
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| The ATPases associated with various cellular activities (AAA) protein p97 has been implicated in a variety of cellular processes, including endoplasmic reticulum-associated degradation and homotypic membrane fusion. p97 belongs to a subgroup of AAA proteins that contains two nucleotide binding domains, D1 and D2. We determined the crystal structure of D2 at 3.0 A resolution. This model enabled rerefinement of full-length p97 in different nucleotide states against previously reported low-resolution diffraction data to significantly improved R values and Ramachandran statistics. Although the overall fold remained similar, there are significant improvements, especially around the D2 nucleotide binding site. The rerefinement illustrates the importance of knowledge of high-resolution structures of fragments covering most of the whole molecule. The structures suggest that nucleotide hydrolysis is transformed into larger conformational changes by pushing of one D2 domain by its neighbor in the hexamer, and transmission of nucleotide-state information through the D1-D2 linker to displace the N-terminal, effector binding domain. | | The line below this paragraph, {{ABSTRACT_PUBMED_18462676}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18462676 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18462676}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Transport protein]] | | [[Category: Transport protein]] |
| [[Category: Ubl conjugation pathway]] | | [[Category: Ubl conjugation pathway]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:37:00 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:06:47 2008'' |