The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Enzyme Structure with Two Catalytic Sites for Double-Sieve Selection of Substrate
Abstract
High-fidelity transfers of genetic information in the central dogma can be achieved by a reaction called editing. The crystal structure of an enzyme with editing activity in translation is presented here at 2.5 angstroms resolution. The enzyme, isoleucyl–transfer RNA synthetase, activates not only the cognate substrate l -isoleucine but also the minimally distinct l -valine in the first, aminoacylation step. Then, in a second, “editing” step, the synthetase itself rapidly hydrolyzes only the valylated products. For this two-step substrate selection, a “double-sieve” mechanism has already been proposed. The present crystal structures of the synthetase in complexes with l -isoleucine and l -valine demonstrate that the first sieve is on the aminoacylation domain containing the Rossmann fold, whereas the second, editing sieve exists on a globular β-barrel domain that protrudes from the aminoacylation domain.
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[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,965
Jones, T. A., Zou, J. Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,648
Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
Eriani, G., Delarue, M., Poch, O., Gangloff, J., & Moras, D. (1990) · Nature · doi:10.1038/347203a0 · Cited by 1,380
[2] Families of serine peptidases
Rawlings, N. D., & Barrett, A. J. (1994) · Methods in Enzymology · doi:10.1016/0076-6879(94)44004-2 · Cited by 629
Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution
Strynadka, N. C. J., Adachi, H., Jensen, S. E., Johns, K., Sielecki, A., Betzel, C., Sutoh, K., & James, M. N. G. (1992) · Nature · doi:10.1038/359700a0 · Cited by 525
Baldwin, A. N., & Berg, P. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96841-9 · Cited by 299
Zhang, Z., Fasco, M. J., Huang, L., Guengerich, F. P., & Kaminsky, L. S. (1996) · PubMed · Cited by 139
Metadata
- Authors
- Nureki, O., Vassylyev, D. G., Tateno, M., Shimada, A., Nakama, T., Fukai, S., Konno, M., Hendrickson, T. L., Schimmel, P., & Yokoyama, S.
- Venue
- Science
- Published
- 1998-04-24
- Volume
- 280
- Issue
- 5363
- Pages
- 578-582
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2004416250
- Cited by
- 317
- References
- 14
- FWCI
- 8.22
- Type
- journal article
- Language
- en
- Open access
- closed
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- Nureki, O., Vassylyev, D. G., Tateno, M., Shimada, A., Nakama, T., Fukai, S., Konno, M., Hendrickson, T. L., Schimmel, P., & Yokoyama, S. (1998). Enzyme Structure with Two Catalytic Sites for Double-Sieve Selection of Substrate. Science. https://doi.org/10.1126/science.280.5363.578
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