1i0x

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(New page: 200px<br /><applet load="1i0x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i0x, resolution 1.65&Aring;" /> '''RIBONUCLEASE T1 IN C...)
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[[Image:1i0x.jpg|left|200px]]<br /><applet load="1i0x" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1i0x, resolution 1.65&Aring;" />
caption="1i0x, resolution 1.65&Aring;" />
'''RIBONUCLEASE T1 IN COMPLEX WITH 2'GMP (FORM II CRYSTAL)'''<br />
'''RIBONUCLEASE T1 IN COMPLEX WITH 2'GMP (FORM II CRYSTAL)'''<br />
==Overview==
==Overview==
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In the crystalline state, ribonuclease T1 binds calcium ions at different, lattice-dependent positions. In solution, its conformational stability is, also remarkably increased in the presence of divalent metal ions., Combining urea unfolding studies and X-ray crystallography, we compared, the presence of several metal ions at specific sites in the protein to, their contribution to the overall stabilizing effect in solution. We, constructed thermodynamic cycles involving particular metal ions and, specific carboxylate functions. The resulting coupling energies indicate, that some (but not all) metal ions found at lattice contacts in crystal, structures may indeed significantly contribute to stability enhancement in, the presence of metal ions in solution.
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In the crystalline state, ribonuclease T1 binds calcium ions at different lattice-dependent positions. In solution, its conformational stability is also remarkably increased in the presence of divalent metal ions. Combining urea unfolding studies and X-ray crystallography, we compared the presence of several metal ions at specific sites in the protein to their contribution to the overall stabilizing effect in solution. We constructed thermodynamic cycles involving particular metal ions and specific carboxylate functions. The resulting coupling energies indicate that some (but not all) metal ions found at lattice contacts in crystal structures may indeed significantly contribute to stability enhancement in the presence of metal ions in solution.
==About this Structure==
==About this Structure==
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1I0X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with CA and 2GP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I0X OCA].
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1I0X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=2GP:'>2GP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I0X OCA].
==Reference==
==Reference==
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[[Category: Loris, R.]]
[[Category: Loris, R.]]
[[Category: Steyaert, J.]]
[[Category: Steyaert, J.]]
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[[Category: Swarte, J.De.]]
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[[Category: Swarte, J De.]]
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[[Category: Vos, S.De.]]
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[[Category: Vos, S De.]]
[[Category: 2GP]]
[[Category: 2GP]]
[[Category: CA]]
[[Category: CA]]
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[[Category: stability]]
[[Category: stability]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:57:44 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:50 2008''

Revision as of 11:06, 21 February 2008


1i0x, resolution 1.65Å

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RIBONUCLEASE T1 IN COMPLEX WITH 2'GMP (FORM II CRYSTAL)

Overview

In the crystalline state, ribonuclease T1 binds calcium ions at different lattice-dependent positions. In solution, its conformational stability is also remarkably increased in the presence of divalent metal ions. Combining urea unfolding studies and X-ray crystallography, we compared the presence of several metal ions at specific sites in the protein to their contribution to the overall stabilizing effect in solution. We constructed thermodynamic cycles involving particular metal ions and specific carboxylate functions. The resulting coupling energies indicate that some (but not all) metal ions found at lattice contacts in crystal structures may indeed significantly contribute to stability enhancement in the presence of metal ions in solution.

About this Structure

1I0X is a Single protein structure of sequence from Aspergillus oryzae with and as ligands. Active as Ribonuclease T(1), with EC number 3.1.27.3 Full crystallographic information is available from OCA.

Reference

The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution., Deswarte J, De Vos S, Langhorst U, Steyaert J, Loris R, Eur J Biochem. 2001 Jul;268(14):3993-4000. PMID:11453993

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