1t8b: Difference between revisions

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[[Image:1t8b.jpg|left|200px]]<br /><applet load="1t8b" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1t8b.jpg|left|200px]]<br /><applet load="1t8b" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1t8b, resolution 3.23Å" />

'''Crystal structure of refolded PHOU-like protein (gi 2983430) from Aquifex aeolicus'''<br />

==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.

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==

1T8B 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1T8B OCA].

1T8B 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=1T8B OCA].

==Reference==

Line 13:

[[Category: Aquifex aeolicus]]

[[Category: Single protein]]

[[Category: Adams, P.D.]]

[[Category: Adams, P D.]]

[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]

[[Category: BSGC, Berkeley Structural Genomics Center.]]

[[Category: Jancarik, J.]]

[[Category: Kim, R.]]

[[Category: Kim, S.H.]]

[[Category: Kim, S H.]]

[[Category: Oganesyan, N.]]

[[Category: Oganesyan, V.]]

Line 27:

[[Category: structural genomics]]

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@@ Line 1: / Line 1: @@
-[[Image:1t8b.jpg|left|200px]]<br /><applet load="1t8b" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1t8b.jpg|left|200px]]<br /><applet load="1t8b" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1t8b, resolution 3.23&Aring;" />
 '''Crystal structure of refolded PHOU-like protein (gi 2983430) from Aquifex aeolicus'''<br />
 ==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.
+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==
-T8B 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T8B OCA].
+T8B 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=1T8B OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Aquifex aeolicus]]
 [[Category: Single protein]]
-[[Category: Adams, P.D.]]
+[[Category: Adams, P D.]]
-[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]
+[[Category: BSGC, Berkeley Structural Genomics Center.]]
 [[Category: Jancarik, J.]]
 [[Category: Kim, R.]]
-[[Category: Kim, S.H.]]
+[[Category: Kim, S H.]]
 [[Category: Oganesyan, N.]]
 [[Category: Oganesyan, V.]]
@@ Line 27: / Line 27: @@
 [[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:03:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:59 2008''