This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1wlf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
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 (&lt;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

Image:1wlf.png

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wlf"
Personal tools