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1i0v

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(New page: 200px<br /><applet load="1i0v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i0v, resolution 1.234&Aring;" /> '''Ribonuclease T1 in ...)
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Revision as of 14:50, 20 November 2007

Image:1i0v.jpg

1i0v, resolution 1.234Å

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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 with CA and 2GP 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 Tue Nov 20 16:57:40 2007

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