Determination of the NMR Structure of Gln25-Ribonuclease T1
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| 024 | 7 | 0 | |a 10.1515/BC.2003.130 |2 doi |
| 035 | |a (NATIONALLICENCE)gruyter-10.1515/BC.2003.130 | ||
| 245 | 0 | 0 | |a Determination of the NMR Structure of Gln25-Ribonuclease T1 |h [Elektronische Daten] |c [K.-i. Hatano, M. Kojima, E.-i. Suzuki, M. Tanokura, K. Takahashi] |
| 520 | 3 | |a 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 threedimensional 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 abovementioned 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. | |
| 540 | |a Copyright © 2003 by Walter de Gruyter GmbH & Co. KG | ||
| 690 | 7 | |a Biochemistry |2 nationallicence | |
| 690 | 7 | |a Molecular biology |2 nationallicence | |
| 690 | 7 | |a Cellular biology |2 nationallicence | |
| 700 | 1 | |a Hatano |D K.-i |4 aut | |
| 700 | 1 | |a Kojima |D M. |4 aut | |
| 700 | 1 | |a Suzuki |D E.-i |4 aut | |
| 700 | 1 | |a Tanokura |D M. |4 aut | |
| 700 | 1 | |a Takahashi |D K. |4 aut | |
| 773 | 0 | |t Biological Chemistry |d Walter de Gruyter |g 384/8(2003-08-20), 1173-1183 |x 1431-6730 |q 384:8<1173 |1 2003 |2 384 |o bchm | |
| 856 | 4 | 0 | |u https://doi.org/10.1515/BC.2003.130 |q text/html |z Onlinezugriff via DOI |
| 908 | |D 1 |a research article |2 jats | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1515/BC.2003.130 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Hatano |D K.-i |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Kojima |D M. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Suzuki |D E.-i |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Tanokura |D M. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Takahashi |D K. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Biological Chemistry |d Walter de Gruyter |g 384/8(2003-08-20), 1173-1183 |x 1431-6730 |q 384:8<1173 |1 2003 |2 384 |o bchm | ||
| 900 | 7 | |b CC0 |u http://creativecommons.org/publicdomain/zero/1.0 |2 nationallicence | |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-gruyter | ||