1wlf
From Proteopedia
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'''Structure of the N-terminal domain of PEX1 AAA-ATPase: Characterization of a putative adaptor-binding domain''' | '''Structure of the N-terminal domain of PEX1 AAA-ATPase: Characterization of a putative adaptor-binding domain''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLF OCA]. | |
==Reference== | ==Reference== | ||
Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain., Shiozawa K, Maita N, Tomii K, Seto A, Goda N, Akiyama Y, Shimizu T, Shirakawa M, Hiroaki H, J Biol Chem. 2004 Nov 26;279(48):50060-8. Epub 2004 Aug 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15328346 15328346] | Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain., Shiozawa K, Maita N, Tomii K, Seto A, Goda N, Akiyama Y, Shimizu T, Shirakawa M, Hiroaki H, J Biol Chem. 2004 Nov 26;279(48):50060-8. Epub 2004 Aug 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15328346 15328346] | ||
| - | [[Category: Mus musculus]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Akiyama, Y.]] | [[Category: Akiyama, Y.]] | ||
[[Category: Goda, N.]] | [[Category: Goda, N.]] | ||
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[[Category: Tochio, H.]] | [[Category: Tochio, H.]] | ||
[[Category: Tomii, K.]] | [[Category: Tomii, K.]] | ||
| - | [[Category: | + | [[Category: N-terminal domain]] |
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Revision as of 10:50, 3 May 2008
Structure of the N-terminal domain of PEX1 AAA-ATPase: Characterization of a putative adaptor-binding domain
Overview
Peroxisomes are responsible for several pathways in primary metabolism, including beta-oxidation and lipid biosynthesis. PEX1 and PEX6 are hexameric AAA-type ATPases, both of which are indispensable in targeting over 50 peroxisomal resident proteins from the cytosol to the peroxisomes. Although the tandem AAA-ATPase domains in the central region of PEX1 and PEX6 are highly similar, the N-terminal sequences are unique. To better understand the distinct molecular function of these two proteins, we analyzed the unique N-terminal domain (NTD) of PEX1. Extensive computational analysis revealed weak similarity (<10% identity) of PEX1 NTD to the N-terminal domains of other membrane-related type II AAA-ATPases, such as VCP (p97) and NSF. We have determined the crystal structure of mouse PEX1 NTD at 2.05-A resolution, which clearly demonstrated that the domain belongs to the double-psi-barrel fold family found in the other AAA-ATPases. The N-domains of both VCP and NSF are structural neighbors of PEX1 NTD with a 2.7- and 2.1-A root mean square deviation of backbone atoms, respectively. Our findings suggest that the supradomain architecture, which is composed of a single N-terminal domain followed by tandem AAA domains, is a common feature of organellar membrane-associating AAA-ATPases. We propose that PEX1 functions as a protein unfoldase in peroxisomal biogenesis, using its N-terminal putative adaptor-binding domain.
About this Structure
Full crystallographic information is available from OCA.
Reference
Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain., Shiozawa K, Maita N, Tomii K, Seto A, Goda N, Akiyama Y, Shimizu T, Shirakawa M, Hiroaki H, J Biol Chem. 2004 Nov 26;279(48):50060-8. Epub 2004 Aug 24. PMID:15328346 Page seeded by OCA on Sat May 3 13:50:17 2008
