Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression

Anat Bashan; Ilana Agmon; Raz Zarivach; Frank Schluenzen; Joerg Harms; Rita Berisio; Heike Bartels; Francois Franceschi; Tamar Auerbach; Harly A.S. Hansen; Elizaveta Kossoy; Maggie Kessler; Ada Yonath

doi:10.1016/S1097-2765(03)00009-1

Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression

Anat Bashan, Ilana Agmon, Raz Zarivach, Frank Schluenzen, Joerg Harms, Rita Berisio, Heike Bartels, Francois Franceschi, Tamar Auerbach, Harly A.S. Hansen, Elizaveta Kossoy, Maggie Kessler, Ada Yonath

Research output: Contribution to journal › Article › peer-review

253 Scopus citations

Abstract

Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3′ end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this mechanism.

Original language	English
Pages (from-to)	91-102
Number of pages	12
Journal	Molecular Cell
Volume	11
Issue number	1
DOIs	https://doi.org/10.1016/S1097-2765(03)00009-1
State	Published - 1 Jan 2003
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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Bashan, A., Agmon, I., Zarivach, R., Schluenzen, F., Harms, J., Berisio, R., Bartels, H., Franceschi, F., Auerbach, T., Hansen, H. A. S., Kossoy, E., Kessler, M., & Yonath, A. (2003). Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression. Molecular Cell, 11(1), 91-102. https://doi.org/10.1016/S1097-2765(03)00009-1

@article{fac33bdf8ca540469fd34ed511795955,

title = "Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression",

abstract = "Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3′ end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this mechanism.",

author = "Anat Bashan and Ilana Agmon and Raz Zarivach and Frank Schluenzen and Joerg Harms and Rita Berisio and Heike Bartels and Francois Franceschi and Tamar Auerbach and Hansen, {Harly A.S.} and Elizaveta Kossoy and Maggie Kessler and Ada Yonath",

note = "Funding Information: We thank J.M. Lehn, M. Lahav, P. Fucini, A. Mankin, and W. Traub for critical discussions; R. Albrecht, D. Baram, W.S. Bennett, E. Ben-Zeev, H. Burmeister, R. Chen, C. Glotz, M. Laschever, C. Liebe, M. Peretz, C. Stamer, and A. Wolff for contributing to these studies; and the staff of ID19/SBC7APS/ANL and ID14-2 and ID14-4/ESRF/EMBL for their cooperation and assistance. The Max-Planck Society, the US National Institutes of Health (GM34360), the German Ministry for Science and Technology (BMBF Grant 05-641EA), and the Kimmelman Center for Macromolecular Assembly at the Weizmann Institute provided support. A.Y. holds the Helen and Martin Kimmel Professorial Chair. ",

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doi = "10.1016/S1097-2765(03)00009-1",

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Bashan, A, Agmon, I, Zarivach, R, Schluenzen, F, Harms, J, Berisio, R, Bartels, H, Franceschi, F, Auerbach, T, Hansen, HAS, Kossoy, E, Kessler, M & Yonath, A 2003, 'Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression', Molecular Cell, vol. 11, no. 1, pp. 91-102. https://doi.org/10.1016/S1097-2765(03)00009-1

TY - JOUR

T1 - Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression

AU - Bashan, Anat

AU - Agmon, Ilana

AU - Zarivach, Raz

AU - Schluenzen, Frank

AU - Harms, Joerg

AU - Berisio, Rita

AU - Bartels, Heike

AU - Franceschi, Francois

AU - Auerbach, Tamar

AU - Hansen, Harly A.S.

AU - Kossoy, Elizaveta

AU - Kessler, Maggie

AU - Yonath, Ada

N1 - Funding Information: We thank J.M. Lehn, M. Lahav, P. Fucini, A. Mankin, and W. Traub for critical discussions; R. Albrecht, D. Baram, W.S. Bennett, E. Ben-Zeev, H. Burmeister, R. Chen, C. Glotz, M. Laschever, C. Liebe, M. Peretz, C. Stamer, and A. Wolff for contributing to these studies; and the staff of ID19/SBC7APS/ANL and ID14-2 and ID14-4/ESRF/EMBL for their cooperation and assistance. The Max-Planck Society, the US National Institutes of Health (GM34360), the German Ministry for Science and Technology (BMBF Grant 05-641EA), and the Kimmelman Center for Macromolecular Assembly at the Weizmann Institute provided support. A.Y. holds the Helen and Martin Kimmel Professorial Chair.

PY - 2003/1/1

Y1 - 2003/1/1

N2 - Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3′ end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this mechanism.

AB - Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3′ end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this mechanism.

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U2 - 10.1016/S1097-2765(03)00009-1

DO - 10.1016/S1097-2765(03)00009-1

M3 - Article

AN - SCOPUS:0037249473

SN - 1097-2765

VL - 11

SP - 91

EP - 102

JO - Molecular Cell

JF - Molecular Cell

IS - 1

ER -

Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression

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