2gza

From Proteopedia

(Difference between revisions)

@@ Line 15: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gz/2gza_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gz/2gza_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 18:50, 24 January 2018

Crystal structure of the VirB11 ATPase from the Brucella Suis type IV secretion system in complex with sulphate

spinqualitylabelsall models

2gza, resolution 2.60Å

Show:Asymmetric Unit Biological Assembly

Drag the structure with the mouse to rotate

Export Animated Image

Structural highlights

2gza is a 3 chain structure with sequence from Brusu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	VirB11 (BRUSU)
Activity:	H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VIRBB_BRUSU] The VirB system could be required for the establishment of the replication niche in the host.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

VirB11 ATPases are hexameric assemblies that power type IV secretion systems in bacteria. The hexamer of Brucella suis VirB11 (BsB11), like that of the Helicobacter pylori VirB11 (Hp0525), consists of a double ring structure formed by the N-terminal and C-terminal domains of each monomer. However, the monomer differs dramatically from that of Hp0525 by a large domain swap that leaves the hexameric assembly intact but profoundly alters the nucleotide-binding site and the interface between subunits.

A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact.,Hare S, Bayliss R, Baron C, Waksman G J Mol Biol. 2006 Jun 30;360(1):56-66. Epub 2006 May 11. PMID:16730027^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hare S, Bayliss R, Baron C, Waksman G. A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact. J Mol Biol. 2006 Jun 30;360(1):56-66. Epub 2006 May 11. PMID:16730027 doi:10.1016/j.jmb.2006.04.060

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2gza"

2gza

From Proteopedia

Revision as of 18:50, 24 January 2018

Crystal structure of the VirB11 ATPase from the Brucella Suis type IV secretion system in complex with sulphate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox