Abstract
Structures of a semisynthetic RNase have been obtained to a resolution of 2.0 Å at pH values of 5.2, 6.5, 7.5, and 8.8, respectively. The principle structural transformation occurring over this pH range is the conversion of the side chain of active site residue His‐119 from one conformation (X 1 = −43° to −57°) at low pH to another (X 1 = + 159° to + 168°) at higher pH values. On the basis of this observation, a model is proposed that reconciles the disparate pK values for His‐119 in the enzyme‐substrate complex that have been deduced from kinetic studies and from proton NMR measurements in the presence of pseudosubstrates.
References
49
Referenced
19
10.1107/S0567740882008346
10.1021/bi00280a021
10.1016/S0021-9258(18)47678-8
10.1021/bi00456a012
10.1021/bi00164a004
10.1021/bi00084a010
10.1016/0167-4838(87)90039-2
10.1006/jmbi.1993.1075
10.1007/BF01875521
- 1971 Academic Press New York F.M. Richards H.W. Wyckoff P.D. Boyer The Enzymes 647 806
- 1982 Academic Press New York P. Blackburn S. Moore P.D. Boyer The Enzymes 317 433
10.1111/j.1749-6632.1986.tb48046.x
10.1021/ja00044a040
10.1073/pnas.82.24.8458
10.1016/S0021-9258(18)48486-4
10.1016/S0021-9258(18)62833-9
10.1016/S0021-9258(19)44976-4
10.1016/S0021-9258(19)44977-6
10.1111/j.1399-3011.1974.tb02401.x
10.1016/S0021-9258(19)41804-8
- 1975 Elsevier Amsterdam R.B. Merrifield R.S. Hodges E.B. Mano Proceedings of the International Symposium on Macromolecules 417 431
10.1002/recl.19800991107
10.1016/0014-5793(84)80498-6
10.1002/recl.19841030203
10.1021/bi00286a021
10.1002/recl.19841031205
10.1073/pnas.88.18.8116
10.1002/pro.5560030106
10.1016/S0022-2836(83)80293-9
10.1016/0003-9861(85)90369-8
10.1016/0022-2836(79)90355-3
10.1107/S0021889887086436
10.1016/S0022-2836(77)80200-3
10.1016/0022-2836(88)90211-2
- 1979 Pergamon Press New York W.A. Hendrickson J.H. Konnert R. Srinivasan Biomolecular Structure Conformation Function and Evolution 43 57
10.1016/0076-6879(85)15014-7
10.1016/0263-7855(87)80024-3
10.1107/S0567739478001618
10.1107/S0021889887087144
10.1016/0022-2836(86)90371-2
10.1016/0022-2836(91)80173-R
10.1016/0141-8130(91)90054-X
10.1016/0022-2836(92)91040-V
10.1042/bj0850127
10.1143/JPSJ.32.1331
10.1016/0022-2836(87)90634-6
10.1042/bj0850152
10.1111/j.1749-6632.1973.tb15296.x
10.1111/j.1432-1033.1978.tb12350.x
Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 5:35 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 8:07 p.m.) |
Indexed | 1 year, 10 months ago (Oct. 16, 2023, 9:13 a.m.) |
Issued | 31 years, 1 month ago (July 25, 1994) |
Published | 31 years, 1 month ago (July 25, 1994) |
Published Online | 23 years, 10 months ago (Oct. 19, 2001) |
Published Print | 31 years, 1 month ago (July 25, 1994) |
@article{J_de_Mel_1994, title={The occupancy of two distinct conformations by active‐site histidine‐119 in crystals of ribonuclease is modulated by pH}, volume={349}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(94)00664-4}, DOI={10.1016/0014-5793(94)00664-4}, number={1}, journal={FEBS Letters}, publisher={Wiley}, author={J. de Mel, V.Srini and Doscher, Marilynn S. and Martin, Philip D. and Edwards, Brian F.P.}, year={1994}, month=jul, pages={155–160} }