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.


1opx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1opx.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1opx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1opx| PDB=1opx | SCENE= }}
{{STRUCTURE_1opx| PDB=1opx | SCENE= }}
-
'''Crystal structure of the traffic ATPase (HP0525) of the Helicobacter pylori type IV secretion system bound by sulfate'''
+
===Crystal structure of the traffic ATPase (HP0525) of the Helicobacter pylori type IV secretion system bound by sulfate===
-
==Overview==
+
<!--
-
The coupling of ATP binding/hydrolysis to macromolecular secretion systems is crucial to the pathogenicity of Gram-negative bacteria. We reported previously the structure of the ADP-bound form of the hexameric traffic VirB11 ATPase of the Helicobacter pylori type IV secretion system (named HP0525), and proposed that it functions as a gating molecule at the inner membrane, cycling through closed and open forms regulated by ATP binding/hydrolysis. Here, we combine crystal structures with analytical ultracentrifugation experiments to show that VirB11 ATPases indeed function as dynamic hexameric assemblies. In the absence of nucleotide, the N-terminal domains exhibit a collection of rigid-body conformations. Nucleotide binding 'locks' the hexamer into a symmetric and compact structure. We propose that VirB11s use the mechanical leverage generated by such nucleotide-dependent conformational changes to facilitate the export of substrates or the assembly of the type IV secretion apparatus. Biochemical characterization of mutant forms of HP0525 coupled with electron microscopy and in vivo assays support such hypothesis, and establish the relevance of VirB11s ATPases as drug targets against pathogenic bacteria.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12727865}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12727865 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12727865}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Sulfate]]
[[Category: Sulfate]]
[[Category: Virb11 atpase]]
[[Category: Virb11 atpase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:08:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:47:58 2008''

Revision as of 10:48, 28 July 2008

Image:1opx.png

Template:STRUCTURE 1opx

Crystal structure of the traffic ATPase (HP0525) of the Helicobacter pylori type IV secretion system bound by sulfate

Template:ABSTRACT PUBMED 12727865

About this Structure

1OPX is a Single protein structure of sequence from Helicobacter pylori 26695. Full crystallographic information is available from OCA.

Reference

VirB11 ATPases are dynamic hexameric assemblies: new insights into bacterial type IV secretion., Savvides SN, Yeo HJ, Beck MR, Blaesing F, Lurz R, Lanka E, Buhrdorf R, Fischer W, Haas R, Waksman G, EMBO J. 2003 May 1;22(9):1969-80. PMID:12727865

Page seeded by OCA on Mon Jul 28 13:47:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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