1IYY
NMR STRUCTURE OF Gln25-RIBONUCLEASE T1, 24 STRUCTURES
Summary for 1IYY
| Entry DOI | 10.2210/pdb1iyy/pdb |
| Related | 1YGW |
| Descriptor | RIBONUCLEASE T1 (1 entity in total) |
| Functional Keywords | ribonuclease, endonuclease, endoribonuclease, hydrolase |
| Biological source | Aspergillus oryzae (Yellow koji mold) |
| Total number of polymer chains | 1 |
| Total formula weight | 11093.64 |
| Authors | Hatano, K.,Kojima, M.,Suzuki, E.,Tanokura, M.,Takahashi, K. (deposition date: 2002-09-12, release date: 2003-10-07, Last modification date: 2024-11-13) |
| Primary citation | Hatano, K.,Kojima, M.,Suzuki, E.,Tanokura, M.,Takahashi, K. Determination of the NMR structure of Gln25-ribonuclease T1. Biol. Chem., 384:1173-1183, 2003 Cited by PubMed Abstract: Ribonuclease (RNase) T1 is a guanyloribonuclease, having two isozymes in nature, Gln25- and Lys25-RNase T1. Between these two isozymes, there is no difference in catalytic activity and three-dimensional structure; however, Lys25-RNase T1 is slightly more stable than Gln25-RNase T1. Recently, it has been suggested that the existence of a salt bridge between Lys25 and Asp29/Glu31 in Lys25-RNase T1 contributes to the stability. To elucidate the effects of the replacement of Lys25 with a Gln on the conformation and microenvironments of RNase T1 in detail, the three-dimensional solution structure of Gln25-RNase T1 was determined by simulated-annealing calculations. As a result, the topology of the overall folding was shown to be very similar to that of the Lys25-isozyme except for some differences. In particular, there were two differences in the property of torsion angles of the two disulfide bonds and the conformations of the residues 11-13, 63-66, and 92-93. With regard to the residues 11-13, the lack of the above-mentioned salt bridge in Gln25-RNase T1 was thought to induce the conformational difference of this segment as compared with the Lys25-isozyme. Furthermore, it was proposed that the perturbation of this segment might transfer to the residues 92-93 via the two disulfide bonds. PubMed: 12974386DOI: 10.1515/BC.2003.130 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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