1js0: Difference between revisions

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[[Image:1js0.gif|left|200px]]<br /><applet load="1js0" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1js0.gif|left|200px]]<br /><applet load="1js0" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1js0, resolution 2.2Å" />

'''Crystal Structure of 3D Domain-swapped RNase A Minor Trimer'''<br />

==Overview==

When concentrated in mildly acidic solutions, bovine pancreatic, ribonuclease (RNase A) forms long-lived oligomers including two types of, dimer, two types of trimer, and higher oligomers. In previous, crystallographic work, we found that the major dimeric component forms by, a swapping of the C-terminal beta-strands between the monomers, and that, the minor dimeric component forms by swapping the N-terminal alpha-helices, of the monomers. On the basis of these structures, we proposed that a, linear RNase A trimer can form from a central molecule that simultaneously, swaps its N-terminal helix with a second RNase A molecule and its, C-terminal strand with a third molecule. Studies by dissociation are, consistent with this model for the major trimeric component: the major, trimer dissociates into both the major and the minor dimers, as well as, monomers. In contrast, the minor trimer component dissociates into the, monomer and the major dimer. This suggests that the minor trimer is, cyclic, formed from three monomers that swap their C-terminal beta-strands, into identical molecules. These conclusions are supported by cross-linking, of lysyl residues, showing that the major trimer swaps its N-terminal, helix, and the minor trimer does not. We verified by X-ray crystallography, the proposed cyclic structure for the minor trimer, with swapping of the, C-terminal beta-strands. This study thus expands the variety of, domain-swapped oligomers by revealing the first example of a protein that, can form both a linear and a cyclic domain-swapped oligomer. These, structures permit interpretation of the enzymatic activities of the RNase, A oligomers on double-stranded RNA.

When concentrated in mildly acidic solutions, bovine pancreatic ribonuclease (RNase A) forms long-lived oligomers including two types of dimer, two types of trimer, and higher oligomers. In previous crystallographic work, we found that the major dimeric component forms by a swapping of the C-terminal beta-strands between the monomers, and that the minor dimeric component forms by swapping the N-terminal alpha-helices of the monomers. On the basis of these structures, we proposed that a linear RNase A trimer can form from a central molecule that simultaneously swaps its N-terminal helix with a second RNase A molecule and its C-terminal strand with a third molecule. Studies by dissociation are consistent with this model for the major trimeric component: the major trimer dissociates into both the major and the minor dimers, as well as monomers. In contrast, the minor trimer component dissociates into the monomer and the major dimer. This suggests that the minor trimer is cyclic, formed from three monomers that swap their C-terminal beta-strands into identical molecules. These conclusions are supported by cross-linking of lysyl residues, showing that the major trimer swaps its N-terminal helix, and the minor trimer does not. We verified by X-ray crystallography the proposed cyclic structure for the minor trimer, with swapping of the C-terminal beta-strands. This study thus expands the variety of domain-swapped oligomers by revealing the first example of a protein that can form both a linear and a cyclic domain-swapped oligomer. These structures permit interpretation of the enzymatic activities of the RNase A oligomers on double-stranded RNA.

==About this Structure==

1JS0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1JS0 OCA].

1JS0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JS0 OCA].

==Reference==

Line 23:

[[Category: rnase a]]

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@@ Line 1: / Line 1: @@
-[[Image:1js0.gif|left|200px]]<br /><applet load="1js0" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1js0.gif|left|200px]]<br /><applet load="1js0" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1js0, resolution 2.2&Aring;" />
 '''Crystal Structure of 3D Domain-swapped RNase A Minor Trimer'''<br />
 ==Overview==
-When concentrated in mildly acidic solutions, bovine pancreatic, ribonuclease (RNase A) forms long-lived oligomers including two types of, dimer, two types of trimer, and higher oligomers. In previous, crystallographic work, we found that the major dimeric component forms by, a swapping of the C-terminal beta-strands between the monomers, and that, the minor dimeric component forms by swapping the N-terminal alpha-helices, of the monomers. On the basis of these structures, we proposed that a, linear RNase A trimer can form from a central molecule that simultaneously, swaps its N-terminal helix with a second RNase A molecule and its, C-terminal strand with a third molecule. Studies by dissociation are, consistent with this model for the major trimeric component: the major, trimer dissociates into both the major and the minor dimers, as well as, monomers. In contrast, the minor trimer component dissociates into the, monomer and the major dimer. This suggests that the minor trimer is, cyclic, formed from three monomers that swap their C-terminal beta-strands, into identical molecules. These conclusions are supported by cross-linking, of lysyl residues, showing that the major trimer swaps its N-terminal, helix, and the minor trimer does not. We verified by X-ray crystallography, the proposed cyclic structure for the minor trimer, with swapping of the, C-terminal beta-strands. This study thus expands the variety of, domain-swapped oligomers by revealing the first example of a protein that, can form both a linear and a cyclic domain-swapped oligomer. These, structures permit interpretation of the enzymatic activities of the RNase, A oligomers on double-stranded RNA.
+When concentrated in mildly acidic solutions, bovine pancreatic ribonuclease (RNase A) forms long-lived oligomers including two types of dimer, two types of trimer, and higher oligomers. In previous crystallographic work, we found that the major dimeric component forms by a swapping of the C-terminal beta-strands between the monomers, and that the minor dimeric component forms by swapping the N-terminal alpha-helices of the monomers. On the basis of these structures, we proposed that a linear RNase A trimer can form from a central molecule that simultaneously swaps its N-terminal helix with a second RNase A molecule and its C-terminal strand with a third molecule. Studies by dissociation are consistent with this model for the major trimeric component: the major trimer dissociates into both the major and the minor dimers, as well as monomers. In contrast, the minor trimer component dissociates into the monomer and the major dimer. This suggests that the minor trimer is cyclic, formed from three monomers that swap their C-terminal beta-strands into identical molecules. These conclusions are supported by cross-linking of lysyl residues, showing that the major trimer swaps its N-terminal helix, and the minor trimer does not. We verified by X-ray crystallography the proposed cyclic structure for the minor trimer, with swapping of the C-terminal beta-strands. This study thus expands the variety of domain-swapped oligomers by revealing the first example of a protein that can form both a linear and a cyclic domain-swapped oligomer. These structures permit interpretation of the enzymatic activities of the RNase A oligomers on double-stranded RNA.
 ==About this Structure==
-JS0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JS0 OCA].
+JS0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JS0 OCA].
 ==Reference==
@@ Line 23: / Line 23: @@
 [[Category: rnase a]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:32:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:05 2008''