2ftk
From Proteopedia
(New page: 200px<br /><applet load="2ftk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ftk, resolution 3.05Å" /> '''berylloflouride Spo0...) |
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| - | [[Image:2ftk.gif|left|200px]]<br /><applet load="2ftk" size=" | + | [[Image:2ftk.gif|left|200px]]<br /><applet load="2ftk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ftk, resolution 3.05Å" /> | caption="2ftk, resolution 3.05Å" /> | ||
'''berylloflouride Spo0F complex with Spo0B'''<br /> | '''berylloflouride Spo0F complex with Spo0B'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A number of regulatory circuits in biological systems function through the | + | A number of regulatory circuits in biological systems function through the exchange of phosphoryl groups from one protein to another. Spo0F and Spo0B are components of a phosphorelay that control sporulation in the bacterium Bacillus subtilis through the exchange of a phosphoryl group. Using beryllofluoride as a mimic for phosphorylation, we trapped the interaction of the phosphorylated Spo0F with Spo0B in the crystal lattice. The transition state of phosphoryl transfer continues to be a highly debated issue, as to whether it is associative or dissociative in nature. The geometry of Spo0F binding to Spo0B favors an associative mechanism for phosphoryl transfer. In order to visualize the autophosphorylation of the histidine kinase, KinA, and the subsequent phosphoryl transfer to Spo0F, we generated in silico models representing these reaction steps. |
==About this Structure== | ==About this Structure== | ||
| - | 2FTK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2FTK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FTK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Varughese, K | + | [[Category: Varughese, K I.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: spo0b phosphorelay]] | [[Category: spo0b phosphorelay]] | ||
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[[Category: sporulation]] | [[Category: sporulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:00 2008'' |
Revision as of 15:25, 21 February 2008
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berylloflouride Spo0F complex with Spo0B
Overview
A number of regulatory circuits in biological systems function through the exchange of phosphoryl groups from one protein to another. Spo0F and Spo0B are components of a phosphorelay that control sporulation in the bacterium Bacillus subtilis through the exchange of a phosphoryl group. Using beryllofluoride as a mimic for phosphorylation, we trapped the interaction of the phosphorylated Spo0F with Spo0B in the crystal lattice. The transition state of phosphoryl transfer continues to be a highly debated issue, as to whether it is associative or dissociative in nature. The geometry of Spo0F binding to Spo0B favors an associative mechanism for phosphoryl transfer. In order to visualize the autophosphorylation of the histidine kinase, KinA, and the subsequent phosphoryl transfer to Spo0F, we generated in silico models representing these reaction steps.
About this Structure
2FTK is a Protein complex structure of sequences from Bacillus subtilis with as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state., Varughese KI, Tsigelny I, Zhao H, J Bacteriol. 2006 Jul;188(13):4970-7. PMID:16788205
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