1i0x

Revision as of 17:50, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1i0x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i0x, resolution 1.65Å" /> '''RIBONUCLEASE T1 IN C...)
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RIBONUCLEASE T1 IN COMPLEX WITH 2'GMP (FORM II CRYSTAL)

File:1i0x.jpg


1i0x, resolution 1.65Å

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OverviewOverview

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 StructureAbout this Structure

1I0X 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.

ReferenceReference

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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