1f0v

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(New page: 200px<br /><applet load="1f0v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f0v, resolution 1.7&Aring;" /> '''Crystal structure of ...)
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[[Image:1f0v.gif|left|200px]]<br /><applet load="1f0v" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1f0v.gif|left|200px]]<br /><applet load="1f0v" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1f0v, resolution 1.7&Aring;" />
caption="1f0v, resolution 1.7&Aring;" />
'''Crystal structure of an Rnase A dimer displaying a new type of 3D domain swapping'''<br />
'''Crystal structure of an Rnase A dimer displaying a new type of 3D domain swapping'''<br />
==Overview==
==Overview==
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Bovine pancreatic ribonuclease (RNase A) forms two types of dimers (a, major and a minor component) upon concentration in mild acid. These two, dimers exhibit different biophysical and biochemical properties. Earlier, we reported that the minor dimer forms by swapping its N-terminal, alpha-helix with that of an identical molecule. Here we find that the, major dimer forms by swapping its C-terminal beta-strand, thus revealing, the first example of three-dimensional (3D) domain swapping taking place, in different parts of the same protein. This feature permits RNase A to, form tightly bonded higher oligomers. The hinge loop of the major dimer, connecting the swapped beta-strand to the protein core, resembles a short, segment of the polar zipper proposed by Perutz and suggests a model for, aggregate formation by 3D domain swapping with a polar zipper.
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Bovine pancreatic ribonuclease (RNase A) forms two types of dimers (a major and a minor component) upon concentration in mild acid. These two dimers exhibit different biophysical and biochemical properties. Earlier we reported that the minor dimer forms by swapping its N-terminal alpha-helix with that of an identical molecule. Here we find that the major dimer forms by swapping its C-terminal beta-strand, thus revealing the first example of three-dimensional (3D) domain swapping taking place in different parts of the same protein. This feature permits RNase A to form tightly bonded higher oligomers. The hinge loop of the major dimer, connecting the swapped beta-strand to the protein core, resembles a short segment of the polar zipper proposed by Perutz and suggests a model for aggregate formation by 3D domain swapping with a polar zipper.
==About this Structure==
==About this Structure==
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1F0V 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 PO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1F0V OCA].
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1F0V 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=PO4:'>PO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1F0V OCA].
==Reference==
==Reference==
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[[Category: Pancreatic ribonuclease]]
[[Category: Pancreatic ribonuclease]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Eisenberg, D.S.]]
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[[Category: Eisenberg, D S.]]
[[Category: Gotte, G.]]
[[Category: Gotte, G.]]
[[Category: Libonati, M.]]
[[Category: Libonati, M.]]
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[[Category: Liu, Y.S.]]
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[[Category: Liu, Y S.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: x-ray]]
[[Category: x-ray]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:30:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:37 2008''

Revision as of 10:33, 21 February 2008


1f0v, resolution 1.7Å

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Crystal structure of an Rnase A dimer displaying a new type of 3D domain swapping

Overview

Bovine pancreatic ribonuclease (RNase A) forms two types of dimers (a major and a minor component) upon concentration in mild acid. These two dimers exhibit different biophysical and biochemical properties. Earlier we reported that the minor dimer forms by swapping its N-terminal alpha-helix with that of an identical molecule. Here we find that the major dimer forms by swapping its C-terminal beta-strand, thus revealing the first example of three-dimensional (3D) domain swapping taking place in different parts of the same protein. This feature permits RNase A to form tightly bonded higher oligomers. The hinge loop of the major dimer, connecting the swapped beta-strand to the protein core, resembles a short segment of the polar zipper proposed by Perutz and suggests a model for aggregate formation by 3D domain swapping with a polar zipper.

About this Structure

1F0V is a Single protein structure of sequence from Bos taurus with and as ligands. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.

Reference

A domain-swapped RNase A dimer with implications for amyloid formation., Liu Y, Gotte G, Libonati M, Eisenberg D, Nat Struct Biol. 2001 Mar;8(3):211-4. PMID:11224563

Page seeded by OCA on Thu Feb 21 12:33:37 2008

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