1WLF

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

Summary for 1WLF

• Entry DOI: 10.2210/pdb1wlf/pdb
• Descriptor: Peroxisome biogenesis factor 1, SULFATE ION (3 entities in total)
• Functional Keywords: n-terminal domain, protein transport
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 20087.77

Authors

Shiozawa, K.,Maita, N.,Tomii, K.,Seto, A.,Goda, N.,Tochio, H.,Akiyama, Y.,Shimizu, T.,Shirakawa, M.,Hiroaki, H. (deposition date: 2004-06-25, release date: 2004-09-07, Last modification date: 2024-03-13)

Primary citation

Shiozawa, K.,Maita, N.,Tomii, K.,Seto, A.,Goda, N.,Akiyama, Y.,Shimizu, T.,Shirakawa, M.,Hiroaki, H.
Structure of the N-terminal Domain of PEX1 AAA-ATPase: CHARACTERIZATION OF A PUTATIVE ADAPTOR-BINDING DOMAIN
J.Biol.Chem., 279:50060-50068, 2004

PubMed Abstract: 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.

PubMed: 15328346
DOI: 10.1074/jbc.M407837200

Experimental method

X-RAY DIFFRACTION (2.05 Å)