1g4a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1g4a.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1g4a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1g4a| PDB=1g4a | SCENE= }}
{{STRUCTURE_1g4a| PDB=1g4a | SCENE= }}
-
'''CRYSTAL STRUCTURES OF THE HSLVU PEPTIDASE-ATPASE COMPLEX REVEAL AN ATP-DEPENDENT PROTEOLYSIS MECHANISM'''
+
===CRYSTAL STRUCTURES OF THE HSLVU PEPTIDASE-ATPASE COMPLEX REVEAL AN ATP-DEPENDENT PROTEOLYSIS MECHANISM===
-
==Overview==
+
<!--
-
BACKGROUND: The bacterial heat shock locus HslU ATPase and HslV peptidase together form an ATP-dependent HslVU protease. Bacterial HslVU is a homolog of the eukaryotic 26S proteasome. Crystallographic studies of HslVU should provide an understanding of ATP-dependent protein unfolding, translocation, and proteolysis by this and other ATP-dependent proteases. RESULTS: We present a 3.0 A resolution crystal structure of HslVU with an HslU hexamer bound at one end of an HslV dodecamer. The structure shows that the central pores of the ATPase and peptidase are next to each other and aligned. The central pore of HslU consists of a GYVG motif, which is conserved among protease-associated ATPases. The binding of one HslU hexamer to one end of an HslV dodecamer in the 3.0 A resolution structure opens both HslV central pores and induces asymmetric changes in HslV. CONCLUSIONS: Analysis of nucleotide binding induced conformational changes in the current and previous HslU structures suggests a protein unfolding-coupled translocation mechanism. In this mechanism, unfolded polypeptides are threaded through the aligned pores of the ATPase and peptidase and translocated into the peptidase central chamber.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11250202}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11250202 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11250202}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[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 17:07:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:23:32 2008''

Revision as of 01:23, 1 July 2008

Image:1g4a.png

Template:STRUCTURE 1g4a

CRYSTAL STRUCTURES OF THE HSLVU PEPTIDASE-ATPASE COMPLEX REVEAL AN ATP-DEPENDENT PROTEOLYSIS MECHANISM

Template:ABSTRACT PUBMED 11250202

About this Structure

1G4A is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism., Wang J, Song JJ, Franklin MC, Kamtekar S, Im YJ, Rho SH, Seong IS, Lee CS, Chung CH, Eom SH, Structure. 2001 Feb 7;9(2):177-84. PMID:11250202

Page seeded by OCA on Tue Jul 1 04:23:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://proteopedia.org/wiki/index.php/1g4a"
Personal tools