Publications
2000
Nikulin A, Serganov A, Ennifar E, Tishchenko S, Nevskaya N, Shepard W, Portier C, Garber M, Ehresmann B, Ehresmann C, Nikonov S, Dumas P
Crystal structure of the S15-rRNA complex Article de journal
Dans: Nat Struct Biol, vol. 7, no. 4, p. 273-277, 2000, ISBN: 10742169, (1072-8368 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: 16S/*chemistry/genetics/*metabolism Ribosomal Proteins/*chemistry/*metabolism Structure-Activity Relationship Support, Amino Acid Sequence Base Pairing/drug effects/genetics Base Sequence Binding Sites/drug effects Conserved Sequence/genetics Crystallography, Bacterial/chemistry/genetics/metabolism RNA, ENNIFAR, Molecular Molecular Sequence Data *Nucleic Acid Conformation/drug effects Protein Conformation RNA, Non-U.S. Gov't Thermus thermophilus/*chemistry/genetics, Ribosomal, Unité ARN, X-Ray Magnesium/pharmacology Models
@article{,
title = {Crystal structure of the S15-rRNA complex},
author = {A Nikulin and A Serganov and E Ennifar and S Tishchenko and N Nevskaya and W Shepard and C Portier and M Garber and B Ehresmann and C Ehresmann and S Nikonov and P Dumas},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10742169},
isbn = {10742169},
year = {2000},
date = {2000-01-01},
journal = {Nat Struct Biol},
volume = {7},
number = {4},
pages = {273-277},
abstract = {In bacterial ribosomes, the small (30S) ribosomal subunit is composed of 16S rRNA and 21 distinct proteins. Ribosomal protein S15 is of particular interest because it binds primarily to 16S rRNA and is required for assembly of the small subunit and for intersubunit association, thus representing a key element in the assembly of a whole ribosome. Here we report the 2.8 inverted question mark resolution crystal structure of the highly conserved S15-rRNA complex. Protein S15 interacts in the minor groove with a G-U/G-C motif and a three-way junction. The latter is constrained by a conserved base triple and stacking interactions, and locked into place by magnesium ions and protein side chains, mainly through interactions with the unique three-dimensional geometry of the backbone. The present structure gives insights into the dual role of S15 in ribosome assembly and translational regulation.},
note = {1072-8368
Journal Article},
keywords = {16S/*chemistry/genetics/*metabolism Ribosomal Proteins/*chemistry/*metabolism Structure-Activity Relationship Support, Amino Acid Sequence Base Pairing/drug effects/genetics Base Sequence Binding Sites/drug effects Conserved Sequence/genetics Crystallography, Bacterial/chemistry/genetics/metabolism RNA, ENNIFAR, Molecular Molecular Sequence Data *Nucleic Acid Conformation/drug effects Protein Conformation RNA, Non-U.S. Gov't Thermus thermophilus/*chemistry/genetics, Ribosomal, Unité ARN, X-Ray Magnesium/pharmacology Models},
pubstate = {published},
tppubtype = {article}
}