2ea1
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(New page: 200px<br /><applet load="2ea1" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ea1, resolution 1.80Å" /> '''Crystal structure of...)
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Revision as of 08:48, 23 January 2008
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Crystal structure of Ribonuclease I from Escherichia coli COMPLEXED WITH GUANYLYL-2(PRIME),5(PRIME)-GUANOSINE
Overview
We have constructed a strain that overproduces ribonuclease I of, Escherichia coli and we have purified large quantities of the enzyme. Data, from fluorescence, CD, and DSC measurements showed that it was a very, stable protein. The conformation energy determined from urea and guanidine, hydrochloride denaturation experiments was 11.5 kcal mol(-1) at pH 7.5., Thermal denaturation studies indicated that it had a T(m) of 64 degrees C, at pH 4.0. RNase I belongs to the RNase T2/S-RNase group of, endoribonucleases, but near the amino terminus it has an unusually long, hydrophilic segment. Part of this was removed in the deletion construct, RNase I Delta(26-38). We have obtained crystals of both RNase I and of an, enzyme-G2'p5'G complex in the P2(1) space group and oligonucleotide, complexes with both wild type and mutant enzymes. The current study lays, the groundwork for extensive investigation into the structure, function, and physical properties of this widely distributed group of ribonucleases.
About this Structure
2EA1 is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Enterobacter ribonuclease, with EC number 3.1.27.6 Full crystallographic information is available from OCA.
Reference
Overexpression, biophysical characterization, and crystallization of ribonuclease I from Escherichia coli, a broad-specificity enzyme in the RNase T2 family., Padmanabhan S, Zhou K, Chu CY, Lim RW, Lim LW, Arch Biochem Biophys. 2001 Jun 1;390(1):42-50. PMID:11368513
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