1nly
From Proteopedia
(New page: 200px<br /><applet load="1nly" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nly, resolution 2.80Å" /> '''Crystal structure of...) |
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| - | [[Image:1nly.jpg|left|200px]]<br /><applet load="1nly" size=" | + | [[Image:1nly.jpg|left|200px]]<br /><applet load="1nly" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nly, resolution 2.80Å" /> | caption="1nly, resolution 2.80Å" /> | ||
'''Crystal structure of the traffic ATPase of the Helicobacter pylori type IV secretion system in complex with ATPgammaS'''<br /> | '''Crystal structure of the traffic ATPase of the Helicobacter pylori type IV secretion system in complex with ATPgammaS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The coupling of ATP binding/hydrolysis to macromolecular secretion systems | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1NLY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695] with MG, SO4, ATG and 2PE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1NLY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ATG:'>ATG</scene> and <scene name='pdbligand=2PE:'>2PE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Helicobacter pylori 26695]] | [[Category: Helicobacter pylori 26695]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Beck, M | + | [[Category: Beck, M R.]] |
[[Category: Blaesing, F.]] | [[Category: Blaesing, F.]] | ||
[[Category: Buhrdorf, R.]] | [[Category: Buhrdorf, R.]] | ||
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[[Category: Lanka, E.]] | [[Category: Lanka, E.]] | ||
[[Category: Lurz, R.]] | [[Category: Lurz, R.]] | ||
| - | [[Category: Savvides, S | + | [[Category: Savvides, S N.]] |
[[Category: Waksman, G.]] | [[Category: Waksman, G.]] | ||
| - | [[Category: Yeo, H | + | [[Category: Yeo, H J.]] |
[[Category: 2PE]] | [[Category: 2PE]] | ||
[[Category: ATG]] | [[Category: ATG]] | ||
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[[Category: virb11 atpase]] | [[Category: virb11 atpase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:30 2008'' |
Revision as of 12:07, 21 February 2008
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Crystal structure of the traffic ATPase of the Helicobacter pylori type IV secretion system in complex with ATPgammaS
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.
About this Structure
1NLY is a Single protein structure of sequence from Helicobacter pylori 26695 with , , and as ligands. 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 Thu Feb 21 14:07:30 2008
Categories: Helicobacter pylori 26695 | Single protein | Beck, M R. | Blaesing, F. | Buhrdorf, R. | Fischer, W. | Haas, R. | Lanka, E. | Lurz, R. | Savvides, S N. | Waksman, G. | Yeo, H J. | 2PE | ATG | MG | SO4 | Atpgammas | Bacterial type iv secretion | Helicobacter pylori | Hp0525 | Virb11 atpase
