1ssc
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(New page: 200px<br /><applet load="1ssc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ssc, resolution 2.0Å" /> '''THE 1.6 ANGSTROMS STR...)
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Revision as of 00:30, 21 November 2007
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THE 1.6 ANGSTROMS STRUCTURE OF A SEMISYNTHETIC RIBONUCLEASE CRYSTALLIZED FROM AQUEOUS ETHANOL. COMPARISON WITH CRYSTALS FROM SALT SOLUTIONS AND WITH RNASE A FROM AQUEOUS ALCOHOL SOLUTIONS
Overview
The non-covalent combination of residues 1-118 of RNase A with a synthetic, 14-residue peptide containing residues 111-124 of the molecule forms a, highly active semisynthetic enzyme, RNase 1-118:111-124. With this enzyme, the roles played by the six C-terminal residues in generating the, catalytic efficiency and substrate specificity of RNase can be studied, using chemically synthesized analogs. The structure of RNase 1-118:111-124, from 43% aqueous ethanol has been determined using molecular-replacement, methods and refined to a crystallographic R-factor of 0.166 for all, observed reflections in the range 7.0-1.6 A (Protein Data Bank file ISSC)., The structure is compared with the 2.0 A structure of RNase A from 43%, aqueous 2-methyl-2-propanol and with the 1.8 A structure of the, semisynthetic enzyme obtained from crystals grown in concentrated salt, solution. The structure of RNase 1-118:111-124 from aqueous ethanol is, virtually identical to that of RNase A from aqueous 2-methyl-2-propanol., Half of the crystallographically bound water molecules are not coincident, however. The structure is somewhat less similar to that of RNase, 1-118:111-124 from salt solutions, with a major difference being the, positioning of active-site residue His119.
About this Structure
1SSC is a Protein complex structure of sequences from Bos taurus with PO4 as ligand. Full crystallographic information is available from OCA.
Reference
1.6 A structure of semisynthetic ribonuclease crystallized from aqueous ethanol. Comparison with crystals from salt solutions and with ribonuclease A from aqueous alcohol solutions., de Mel SJ, Doscher MS, Martin PD, Rodier F, Edwards BF, Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):1003-12. PMID:15299768
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