4ag6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[ | ==Structure of VirB4 of Thermoanaerobacter pseudethanolicus== | ||
<StructureSection load='4ag6' size='340' side='right' caption='[[4ag6]], [[Resolution|resolution]] 2.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ag6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoanaerobacter_pseudethanolicus Thermoanaerobacter pseudethanolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AG6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AG6 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ag5|4ag5]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ag6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ag6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ag6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ag6 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Type IV secretion (T4S) systems mediate the transfer of proteins and DNA across the cell envelope of bacteria. These systems play important roles in bacterial pathogenesis and in horizontal transfer of antibiotic resistance. The VirB4 ATPase of the T4S system is essential for both the assembly of the system and substrate transfer. In this article, we present the crystal structure of the C-terminal domain of Thermoanaerobacter pseudethanolicus VirB4. This structure is strikingly similar to that of another T4S ATPase, VirD4, a protein that shares only 12% sequence identity with VirB4. The VirB4 domain purifies as a monomer, but the full-length protein is observed in a monomer-dimer equilibrium, even in the presence of nucleotides and DNAs. We also report the negative stain electron microscopy structure of the core complex of the T4S system of the Escherichia coli pKM101 plasmid, with VirB4 bound. In this structure, VirB4 is also monomeric and bound through its N-terminal domain to the core's VirB9 protein. Remarkably, VirB4 is observed bound to the side of the complex where it is ideally placed to play its known regulatory role in substrate transfer. | |||
Structure of the VirB4 ATPase, alone and bound to the core complex of a type IV secretion system.,Wallden K, Williams R, Yan J, Lian PW, Wang L, Thalassinos K, Orlova EV, Waksman G Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11348-53. Epub 2012 Jun 27. PMID:22745169<ref>PMID:22745169</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Thermoanaerobacter pseudethanolicus]] | [[Category: Thermoanaerobacter pseudethanolicus]] | ||
[[Category: Lian, P W.]] | [[Category: Lian, P W.]] | ||
Revision as of 11:36, 5 June 2014
Structure of VirB4 of Thermoanaerobacter pseudethanolicusStructure of VirB4 of Thermoanaerobacter pseudethanolicus
Structural highlights
Publication Abstract from PubMedType IV secretion (T4S) systems mediate the transfer of proteins and DNA across the cell envelope of bacteria. These systems play important roles in bacterial pathogenesis and in horizontal transfer of antibiotic resistance. The VirB4 ATPase of the T4S system is essential for both the assembly of the system and substrate transfer. In this article, we present the crystal structure of the C-terminal domain of Thermoanaerobacter pseudethanolicus VirB4. This structure is strikingly similar to that of another T4S ATPase, VirD4, a protein that shares only 12% sequence identity with VirB4. The VirB4 domain purifies as a monomer, but the full-length protein is observed in a monomer-dimer equilibrium, even in the presence of nucleotides and DNAs. We also report the negative stain electron microscopy structure of the core complex of the T4S system of the Escherichia coli pKM101 plasmid, with VirB4 bound. In this structure, VirB4 is also monomeric and bound through its N-terminal domain to the core's VirB9 protein. Remarkably, VirB4 is observed bound to the side of the complex where it is ideally placed to play its known regulatory role in substrate transfer. Structure of the VirB4 ATPase, alone and bound to the core complex of a type IV secretion system.,Wallden K, Williams R, Yan J, Lian PW, Wang L, Thalassinos K, Orlova EV, Waksman G Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11348-53. Epub 2012 Jun 27. PMID:22745169[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||