From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
Line 1: |
Line 1: |
- | [[Image:1wlf.jpg|left|200px]] | + | {{Seed}} |
| + | [[Image:1wlf.png|left|200px]] |
| | | |
| <!-- | | <!-- |
Line 9: |
Line 10: |
| {{STRUCTURE_1wlf| PDB=1wlf | SCENE= }} | | {{STRUCTURE_1wlf| PDB=1wlf | SCENE= }} |
| | | |
- | '''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=== |
| | | |
| | | |
- | ==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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15328346}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 15328346 is the PubMed ID number. |
| + | --> |
| + | {{ABSTRACT_PUBMED_15328346}} |
| | | |
| ==About this Structure== | | ==About this Structure== |
Line 31: |
Line 35: |
| [[Category: Tomii, K.]] | | [[Category: Tomii, K.]] |
| [[Category: N-terminal domain]] | | [[Category: N-terminal domain]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:50:17 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:51:25 2008'' |
Revision as of 17:51, 28 July 2008
Template:STRUCTURE 1wlf
Structure of the N-terminal domain of PEX1 AAA-ATPase: Characterization of a putative adaptor-binding domain
Template:ABSTRACT PUBMED 15328346
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 Mon Jul 28 20:51:25 2008
Categories: Akiyama, Y. | Goda, N. | Hiroaki, H. | Maita, N. | Seto, A. | Shimizu, T. | Shiozawa, K. | Shirakawa, M. | Tochio, H. | Tomii, K. | N-terminal domain