1t72
From Proteopedia
(New page: 200px<br /><applet load="1t72" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t72, resolution 2.9Å" /> '''Crystal structure of ...) |
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| - | [[Image:1t72.gif|left|200px]]<br /><applet load="1t72" size=" | + | [[Image:1t72.gif|left|200px]]<br /><applet load="1t72" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t72, resolution 2.9Å" /> | caption="1t72, resolution 2.9Å" /> | ||
'''Crystal structure of phosphate transport system protein phoU from Aquifex aeolicus'''<br /> | '''Crystal structure of phosphate transport system protein phoU from Aquifex aeolicus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The phoU gene of Aquifex aeolicus encodes a protein called PHOU_AQUAE with | + | The phoU gene of Aquifex aeolicus encodes a protein called PHOU_AQUAE with sequence similarity to the PhoU protein of Escherichia coli. Despite the fact that there is a large number of family members (more than 300) attributed to almost all known bacteria and despite PHOU_AQUAE's association with the regulation of genes for phosphate metabolism, the nature of its regulatory function is not well understood. Nearly one-half of these PhoU-like proteins, including both PHOU_AQUAE and the one from E. coli, form a subfamily with an apparent dimer structure of two PhoU domains on the basis of their amino acid sequence. The crystal structure of PHOU_AQUAE (a 221-amino-acid protein) reveals two similar coiled-coil PhoU domains, each forming a three-helix bundle. The structures of PHOU_AQUAE proteins from both a soluble fraction and refolded inclusion bodies (at resolutions of 2.8 and 3.2A, respectively) showed no significant differences. The folds of the PhoU domain and Bag domains (for a class of cofactors of the eukaryotic chaperone Hsp70 family) are similar. Accordingly, we propose that gene regulation by PhoU may occur by association of PHOU_AQUAE with the ATPase domain of the histidine kinase PhoR, promoting release of its substrate PhoB. Other proteins that share the PhoU domain fold include the coiled-coil domains of the STAT protein, the ribosome-recycling factor, and structural proteins like spectrin. |
==About this Structure== | ==About this Structure== | ||
| - | 1T72 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http:// | + | 1T72 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T72 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Adams, P | + | [[Category: Adams, P D.]] |
| - | [[Category: BSGC, Berkeley | + | [[Category: BSGC, Berkeley Structural Genomics Center.]] |
[[Category: Jancarik, J.]] | [[Category: Jancarik, J.]] | ||
[[Category: Kim, R.]] | [[Category: Kim, R.]] | ||
| - | [[Category: Kim, S | + | [[Category: Kim, S H.]] |
[[Category: Oganesyan, N.]] | [[Category: Oganesyan, N.]] | ||
[[Category: Oganesyan, V.]] | [[Category: Oganesyan, V.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:34 2008'' |
Revision as of 13:10, 21 February 2008
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Crystal structure of phosphate transport system protein phoU from Aquifex aeolicus
Overview
The phoU gene of Aquifex aeolicus encodes a protein called PHOU_AQUAE with sequence similarity to the PhoU protein of Escherichia coli. Despite the fact that there is a large number of family members (more than 300) attributed to almost all known bacteria and despite PHOU_AQUAE's association with the regulation of genes for phosphate metabolism, the nature of its regulatory function is not well understood. Nearly one-half of these PhoU-like proteins, including both PHOU_AQUAE and the one from E. coli, form a subfamily with an apparent dimer structure of two PhoU domains on the basis of their amino acid sequence. The crystal structure of PHOU_AQUAE (a 221-amino-acid protein) reveals two similar coiled-coil PhoU domains, each forming a three-helix bundle. The structures of PHOU_AQUAE proteins from both a soluble fraction and refolded inclusion bodies (at resolutions of 2.8 and 3.2A, respectively) showed no significant differences. The folds of the PhoU domain and Bag domains (for a class of cofactors of the eukaryotic chaperone Hsp70 family) are similar. Accordingly, we propose that gene regulation by PhoU may occur by association of PHOU_AQUAE with the ATPase domain of the histidine kinase PhoR, promoting release of its substrate PhoB. Other proteins that share the PhoU domain fold include the coiled-coil domains of the STAT protein, the ribosome-recycling factor, and structural proteins like spectrin.
About this Structure
1T72 is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the "PhoU-like" phosphate uptake regulator from Aquifex aeolicus., Oganesyan V, Oganesyan N, Adams PD, Jancarik J, Yokota HA, Kim R, Kim SH, J Bacteriol. 2005 Jun;187(12):4238-44. PMID:15937186
Page seeded by OCA on Thu Feb 21 15:10:34 2008
Categories: Aquifex aeolicus | Single protein | Adams, P D. | BSGC, Berkeley Structural Genomics Center. | Jancarik, J. | Kim, R. | Kim, S H. | Oganesyan, N. | Oganesyan, V. | Berkeley structural genomics center | Bsgc structure funded by nih | Helix bundle | Protein structure initiative | Psi | Structural genomics
