1hyf
From Proteopedia
(New page: 200px<br /><applet load="1hyf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hyf, resolution 1.70Å" /> '''RIBONUCLEASE T1 V16A...) |
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| - | [[Image:1hyf.gif|left|200px]]<br /><applet load="1hyf" size=" | + | [[Image:1hyf.gif|left|200px]]<br /><applet load="1hyf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hyf, resolution 1.70Å" /> | caption="1hyf, resolution 1.70Å" /> | ||
'''RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH SR2+'''<br /> | '''RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH SR2+'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In the crystalline state, ribonuclease T1 binds calcium ions at different | + | 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== | ||
| - | 1HYF 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 SR 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:// | + | 1HYF 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=SR:'>SR</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=1HYF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Loris, R.]] | [[Category: Loris, R.]] | ||
[[Category: Steyaert, J.]] | [[Category: Steyaert, J.]] | ||
| - | [[Category: Swarte, J | + | [[Category: Swarte, J De.]] |
| - | [[Category: Vos, S | + | [[Category: Vos, S De.]] |
[[Category: 2GP]] | [[Category: 2GP]] | ||
[[Category: SR]] | [[Category: SR]] | ||
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[[Category: stability]] | [[Category: stability]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:02 2008'' |
Revision as of 11:06, 21 February 2008
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RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH SR2+
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
1HYF 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
Page seeded by OCA on Thu Feb 21 13:06:02 2008
