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.


1ht2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ht2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ht2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ht2| PDB=1ht2 | SCENE= }}
{{STRUCTURE_1ht2| PDB=1ht2 | SCENE= }}
-
'''Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU'''
+
===Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU===
-
==Overview==
+
<!--
-
BACKGROUND: The bacterial heat shock locus ATPase HslU is an AAA(+) protein that has structures known in many nucleotide-free and -bound states. Nucleotide is required for the formation of the biologically active HslU hexameric assembly. The hexameric HslU ATPase binds the dodecameric HslV peptidase and forms an ATP-dependent HslVU protease. RESULTS: We have characterized four distinct HslU conformational states, going sequentially from open to closed: the empty, SO(4), ATP, and ADP states. The nucleotide binds at a cleft formed by an alpha/beta domain and an alpha-helical domain in HslU. The four HslU states differ by a rotation of the alpha-helical domain. This classification leads to a correction of nucleotide identity in one structure and reveals the ATP hydrolysis-dependent structural changes in the HslVU complex, including a ring rotation and a conformational change of the HslU C terminus. This leads to an amended protein unfolding-coupled translocation mechanism. CONCLUSIONS: The observed nucleotide-dependent conformational changes in HslU and their governing principles provide a framework for the mechanistic understanding of other AAA(+) proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11709174}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11709174 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11709174}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Hslvu]]
[[Category: Hslvu]]
[[Category: Peptidase-atpase complex]]
[[Category: Peptidase-atpase complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:12:09 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:38:25 2008''

Revision as of 05:38, 1 July 2008

Image:1ht2.png

Template:STRUCTURE 1ht2

Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU

Template:ABSTRACT PUBMED 11709174

About this Structure

1HT2 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU., Wang J, Song JJ, Seong IS, Franklin MC, Kamtekar S, Eom SH, Chung CH, Structure. 2001 Nov;9(11):1107-16. PMID:11709174

Page seeded by OCA on Tue Jul 1 08:38:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ht2"
Personal tools