1y50: Difference between revisions

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[[Image:1y50.gif|left|200px]]<br /><applet load="1y50" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1y50.gif|left|200px]]<br /><applet load="1y50" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1y50, resolution 2.00Å" />

'''X-ray crystal structure of Bacillus stearothermophilus Histidine phosphocarrier protein (Hpr) F29W mutant domain_swapped dimer'''<br />

==Overview==

The study of proteins from extremophilic organisms continues to generate, interest in the field of protein folding because paradigms explaining the, enhanced stability of these proteins still elude us and such studies have, the potential to further our knowledge of the forces stabilizing proteins., We have undertaken such a study with our model protein HPr from a, mesophile, Bacillus subtilis, and a thermophile, Bacillus, stearothermophilus. We report here the high-resolution structures of the, wild-type HPr protein from the thermophile and a variant, F29W. The, variant proved to crystallize in two forms: a monomeric form with a, structure very similar to the wild-type protein as well as a, domain-swapped dimer. Interestingly, the structure of the domain-swapped, dimer for HPr is very different from that observed for a homologous, protein, Crh, from B.subtilis. The existence of a domain-swapped dimer has, implications for amyloid formation and is consistent with recent results, showing that the HPr proteins can form amyloid fibrils. We also, characterized the conformational stability of the thermophilic HPr, proteins using thermal and solvent denaturation methods and have used the, high-resolution structures in an attempt to explain the differences in, stability between the different HPr proteins. Finally, we present a, detailed analysis of the solution properties of the HPr proteins using a, variety of biochemical and biophysical methods.

The study of proteins from extremophilic organisms continues to generate interest in the field of protein folding because paradigms explaining the enhanced stability of these proteins still elude us and such studies have the potential to further our knowledge of the forces stabilizing proteins. We have undertaken such a study with our model protein HPr from a mesophile, Bacillus subtilis, and a thermophile, Bacillus stearothermophilus. We report here the high-resolution structures of the wild-type HPr protein from the thermophile and a variant, F29W. The variant proved to crystallize in two forms: a monomeric form with a structure very similar to the wild-type protein as well as a domain-swapped dimer. Interestingly, the structure of the domain-swapped dimer for HPr is very different from that observed for a homologous protein, Crh, from B.subtilis. The existence of a domain-swapped dimer has implications for amyloid formation and is consistent with recent results showing that the HPr proteins can form amyloid fibrils. We also characterized the conformational stability of the thermophilic HPr proteins using thermal and solvent denaturation methods and have used the high-resolution structures in an attempt to explain the differences in stability between the different HPr proteins. Finally, we present a detailed analysis of the solution properties of the HPr proteins using a variety of biochemical and biophysical methods.

==About this Structure==

1Y50 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1Y50 OCA].

1Y50 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y50 OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Razvi, A.]]

[[Category: Sacchettini, J.C.]]

[[Category: Sacchettini, J C.]]

[[Category: Scholtz, J.M.]]

[[Category: Scholtz, J M.]]

[[Category: Sridharan, S.]]

[[Category: SO4]]

[[Category: bacillus stearothermophilus f29w mutant domain-swapped dimer]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 06:34:~~17 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:49 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1y50.gif|left|200px]]<br /><applet load="1y50" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1y50.gif|left|200px]]<br /><applet load="1y50" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1y50, resolution 2.00&Aring;" />
 '''X-ray crystal structure of Bacillus stearothermophilus Histidine phosphocarrier protein (Hpr) F29W mutant domain_swapped dimer'''<br />
 ==Overview==
-The study of proteins from extremophilic organisms continues to generate, interest in the field of protein folding because paradigms explaining the, enhanced stability of these proteins still elude us and such studies have, the potential to further our knowledge of the forces stabilizing proteins., We have undertaken such a study with our model protein HPr from a, mesophile, Bacillus subtilis, and a thermophile, Bacillus, stearothermophilus. We report here the high-resolution structures of the, wild-type HPr protein from the thermophile and a variant, F29W. The, variant proved to crystallize in two forms: a monomeric form with a, structure very similar to the wild-type protein as well as a, domain-swapped dimer. Interestingly, the structure of the domain-swapped, dimer for HPr is very different from that observed for a homologous, protein, Crh, from B.subtilis. The existence of a domain-swapped dimer has, implications for amyloid formation and is consistent with recent results, showing that the HPr proteins can form amyloid fibrils. We also, characterized the conformational stability of the thermophilic HPr, proteins using thermal and solvent denaturation methods and have used the, high-resolution structures in an attempt to explain the differences in, stability between the different HPr proteins. Finally, we present a, detailed analysis of the solution properties of the HPr proteins using a, variety of biochemical and biophysical methods.
+The study of proteins from extremophilic organisms continues to generate interest in the field of protein folding because paradigms explaining the enhanced stability of these proteins still elude us and such studies have the potential to further our knowledge of the forces stabilizing proteins. We have undertaken such a study with our model protein HPr from a mesophile, Bacillus subtilis, and a thermophile, Bacillus stearothermophilus. We report here the high-resolution structures of the wild-type HPr protein from the thermophile and a variant, F29W. The variant proved to crystallize in two forms: a monomeric form with a structure very similar to the wild-type protein as well as a domain-swapped dimer. Interestingly, the structure of the domain-swapped dimer for HPr is very different from that observed for a homologous protein, Crh, from B.subtilis. The existence of a domain-swapped dimer has implications for amyloid formation and is consistent with recent results showing that the HPr proteins can form amyloid fibrils. We also characterized the conformational stability of the thermophilic HPr proteins using thermal and solvent denaturation methods and have used the high-resolution structures in an attempt to explain the differences in stability between the different HPr proteins. Finally, we present a detailed analysis of the solution properties of the HPr proteins using a variety of biochemical and biophysical methods.
 ==About this Structure==
-Y50 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y50 OCA].
+Y50 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y50 OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Razvi, A.]]
-[[Category: Sacchettini, J.C.]]
+[[Category: Sacchettini, J C.]]
-[[Category: Scholtz, J.M.]]
+[[Category: Scholtz, J M.]]
 [[Category: Sridharan, S.]]
 [[Category: SO4]]
 [[Category: bacillus stearothermophilus f29w mutant domain-swapped dimer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:34:17 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:49 2008''