2vii
From Proteopedia
(New page: 200px<br /><applet load="2vii" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vii, resolution 2.85Å" /> '''PSPF1-275-MG-AMP'''<...) |
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==Overview== | ==Overview== | ||
| - | Mechanochemical proteins rely on ATP hydrolysis to establish the different | + | Mechanochemical proteins rely on ATP hydrolysis to establish the different functional states required for their biological output. Studying the transient functional intermediate states these proteins adopt as they progress through the ATP hydrolysis cycle is key to understanding the molecular basis of their mechanism. Many of these intermediates have been successfully 'trapped' and functionally characterised using ATP analogues. Here, we present a new nucleotide analogue, AMP-AlF(x), which traps PspF, a bacterial enhancer binding protein, in a stable complex with the sigma(54)-RNA polymerase holoenzyme. The crystal structure of AMP-AlF(x)*PspF(1-275) provides new information on protein-nucleotide interactions and suggests that the beta and gamma phosphates are more important than the alpha phosphate in terms of sensing nucleotide bound states. In addition, functional data obtained with AMP-AlF(x) establish distinct roles for the conserved catalytic AAA(+) (ATPases associated with various cellular activities) residues, suggesting that AMP-AlF(x) is a powerful new tool to study AAA(+) protein family members and, more generally, Walker motif ATPases. |
==About this Structure== | ==About this Structure== | ||
| - | 2VII is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Amp Binding Site For Chain A'>AC1</scene> and <scene name='pdbsite=AC2:Mg Binding Site For Chain A'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VII OCA]. | + | 2VII is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Amp+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Mg+Binding+Site+For+Chain+A'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VII OCA]. |
==Reference== | ==Reference== | ||
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[[Category: two-component regulatory system]] | [[Category: two-component regulatory system]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:56:14 2008'' |
Revision as of 16:56, 21 February 2008
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PSPF1-275-MG-AMP
Overview
Mechanochemical proteins rely on ATP hydrolysis to establish the different functional states required for their biological output. Studying the transient functional intermediate states these proteins adopt as they progress through the ATP hydrolysis cycle is key to understanding the molecular basis of their mechanism. Many of these intermediates have been successfully 'trapped' and functionally characterised using ATP analogues. Here, we present a new nucleotide analogue, AMP-AlF(x), which traps PspF, a bacterial enhancer binding protein, in a stable complex with the sigma(54)-RNA polymerase holoenzyme. The crystal structure of AMP-AlF(x)*PspF(1-275) provides new information on protein-nucleotide interactions and suggests that the beta and gamma phosphates are more important than the alpha phosphate in terms of sensing nucleotide bound states. In addition, functional data obtained with AMP-AlF(x) establish distinct roles for the conserved catalytic AAA(+) (ATPases associated with various cellular activities) residues, suggesting that AMP-AlF(x) is a powerful new tool to study AAA(+) protein family members and, more generally, Walker motif ATPases.
About this Structure
2VII is a Single protein structure of sequence from Escherichia coli with and as ligands. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Trapping of a transcription complex using a new nucleotide analogue: AMP aluminium fluoride., Joly N, Rappas M, Buck M, Zhang X, J Mol Biol. 2008 Feb 1;375(5):1206-11. Epub 2007 Nov 22. PMID:18082766
Page seeded by OCA on Thu Feb 21 18:56:14 2008
Categories: Escherichia coli | Single protein | Buck, M. | Joly, N. | Rappas, M. | Zhang, X. | AMP | MG | Aaa | Activator | Atp-binding | Dna-binding | Enhancer binding protein | Gene regulation | Nucleotide-binding | Pspf | Sigma54 activator | Transcription | Transcription activation | Transcription regulation | Two-component regulatory system
