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1i0v

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|PDB= 1i0v |SIZE=350|CAPTION= <scene name='initialview01'>1i0v</scene>, resolution 1.234&Aring;
|PDB= 1i0v |SIZE=350|CAPTION= <scene name='initialview01'>1i0v</scene>, resolution 1.234&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=2GP:GUANOSINE-2&#39;-MONOPHOSPHATE'>2GP</scene>
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|LIGAND= <scene name='pdbligand=2GP:GUANOSINE-2&#39;-MONOPHOSPHATE'>2GP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1i0x|1I0X]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i0v OCA], [http://www.ebi.ac.uk/pdbsum/1i0v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i0v RCSB]</span>
}}
}}
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[[Category: Swarte, J De.]]
[[Category: Swarte, J De.]]
[[Category: Vos, S De.]]
[[Category: Vos, S De.]]
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[[Category: 2GP]]
 
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[[Category: CA]]
 
[[Category: 2'gmp]]
[[Category: 2'gmp]]
[[Category: metal binding]]
[[Category: metal binding]]
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[[Category: stability]]
[[Category: stability]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:09:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:13:04 2008''

Revision as of 18:13, 30 March 2008


PDB ID 1i0v

Drag the structure with the mouse to rotate
, resolution 1.234Å
Ligands: ,
Activity: Ribonuclease T(1), with EC number 3.1.27.3
Related: 1I0X


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Ribonuclease T1 in complex with 2'GMP (form I 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

1I0V is a Single protein structure of sequence from Aspergillus oryzae. 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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