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1I0X

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

Summary for 1I0X
Entry DOI10.2210/pdb1i0x/pdb
Related1I0V
DescriptorGUANYL-SPECIFIC RIBONUCLEASE T1, GUANOSINE-2'-MONOPHOSPHATE, CALCIUM ION, ... (4 entities in total)
Functional Keywordsribonuclease, rnase, metal binding, stability, 2'gmp, hydrolase
Biological sourceAspergillus oryzae
Total number of polymer chains4
Total formula weight46395.27
Authors
De Swarte, J.,De Vos, S.,Langhorst, U.,Steyaert, J.,Loris, R. (deposition date: 2001-01-30, release date: 2001-02-14, Last modification date: 2021-10-27)
Primary citationDeswarte, J.,De Vos, S.,Langhorst, U.,Steyaert, J.,Loris, R.
The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution.
Eur.J.Biochem., 268:3993-4000, 2001
Cited by
PubMed Abstract: 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.
PubMed: 11453993
DOI: 10.1046/j.1432-1327.2001.02310.x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

227111

數據於2024-11-06公開中

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