1ssc
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
OverviewOverview
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 StructureAbout this Structure
1SSC is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 09:05:08 2008