1HZ1

RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+

Summary for 1HZ1

• Entry DOI: 10.2210/pdb1hz1/pdb
• Descriptor: RIBONUCLEASE T1, MAGNESIUM ION, GUANOSINE-2'-MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: ribonuclease, metal binding, stability, hydrolase
• Biological source: Aspergillus niger
• Total number of polymer chains: 1
• Total formula weight: 11454.17

Authors

De Swarte, J.,De Vos, S.,Langhorst, U.,Steyaert, J.,Loris, R. (deposition date: 2001-01-23, release date: 2001-01-31, Last modification date: 2024-10-30)

Primary citation

Deswarte, 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

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)