1wlf
From Proteopedia
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|PDB= 1wlf |SIZE=350|CAPTION= <scene name='initialview01'>1wlf</scene>, resolution 2.05Å | |PDB= 1wlf |SIZE=350|CAPTION= <scene name='initialview01'>1wlf</scene>, resolution 2.05Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wlf OCA], [http://www.ebi.ac.uk/pdbsum/1wlf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wlf RCSB]</span> | ||
}} | }} | ||
| Line 32: | Line 35: | ||
[[Category: Tochio, H.]] | [[Category: Tochio, H.]] | ||
[[Category: Tomii, K.]] | [[Category: Tomii, K.]] | ||
| - | [[Category: SO4]] | ||
[[Category: n-terminal domain]] | [[Category: n-terminal domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:37:50 2008'' |
Revision as of 21:37, 30 March 2008
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| , resolution 2.05Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1WLF is a Protein complex structure of sequences from Mus musculus. 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
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