MISC

2004年11月

Structure of the N-terminal domain of PEX1 AAA-ATPase - Characterization of a putative adaptor-binding domain

JOURNAL OF BIOLOGICAL CHEMISTRY
  • K Shiozawa
  • ,
  • N Maita
  • ,
  • K Tomii
  • ,
  • A Seto
  • ,
  • N Goda
  • ,
  • Y Akiyama
  • ,
  • T Shimizu
  • ,
  • M Shirakawa
  • ,
  • H Hiroaki

279
48
開始ページ
50060
終了ページ
50068
記述言語
英語
掲載種別
DOI
10.1074/jbc.M407837200
出版者・発行元
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

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-angstrom 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-angstrom 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.

Web of Science ® 被引用回数 : 56

リンク情報
DOI
https://doi.org/10.1074/jbc.M407837200
CiNii Articles
http://ci.nii.ac.jp/naid/30016361395
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/15328346
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000225229500064&DestApp=WOS_CPL
ID情報
  • DOI : 10.1074/jbc.M407837200
  • ISSN : 0021-9258
  • eISSN : 1083-351X
  • CiNii Articles ID : 30016361395
  • PubMed ID : 15328346
  • Web of Science ID : WOS:000225229500064

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