1i0x: Difference between revisions
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|PDB= 1i0x |SIZE=350|CAPTION= <scene name='initialview01'>1i0x</scene>, resolution 1.65Å | |PDB= 1i0x |SIZE=350|CAPTION= <scene name='initialview01'>1i0x</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=2GP:GUANOSINE-2'-MONOPHOSPHATE'>2GP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|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] | |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=[[1i0v|1I0V]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i0x OCA], [http://www.ebi.ac.uk/pdbsum/1i0x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i0x RCSB]</span> | |||
}} | }} | ||
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[[Category: Swarte, J De.]] | [[Category: Swarte, J De.]] | ||
[[Category: Vos, S De.]] | [[Category: Vos, S De.]] | ||
[[Category: 2'gmp]] | [[Category: 2'gmp]] | ||
[[Category: metal binding]] | [[Category: metal binding]] | ||
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[[Category: stability]] | [[Category: stability]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''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
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| 1i0x, resolution 1.65Å | |||||||||||||
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| Ligands: | 2GP, CA | ||||||||||||
| Activity: | Ribonuclease T(1), with EC number 3.1.27.3 | ||||||||||||
| Related: | 1I0V
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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