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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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Fragment-based:
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Template-based:
GeNMR
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Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
CS23D
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Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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From structure:
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From sequence:
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Disordered proteins:
MAXOCC
Format conversion & validation:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
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Isotope labeling:
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Solid-state NMR:
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Old 08-22-2010, 03:01 AM
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Default Ribosomal protein S17: characterization of the three-dimensional structure by 1H and

Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.

Related Articles Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.

Biochemistry. 1993 Nov 30;32(47):12812-20

Authors: Golden BL, Hoffman DW, Ramakrishnan V, White SW

The structure of ribosomal protein S17 from Bacillus stearothermophilus was investigated by two-dimensional homonuclear and heteronuclear magnetic resonance spectroscopy. The 1H and 15N chemical shift assignments are largely complete, and a preliminary structural characterization is presented. The protein consists of five beta-strands that form a single antiparallel beta-sheet with Greek-key topology. The beta-strands are connected by several extended loops, and two of these contain residue types that are frequently seen in the RNA-binding sites of proteins. Additionally, two point mutations that affect antibiotic resistance, translational fidelity, and ribosome assembly are located in these two regions of the protein. Since these potential RNA-binding sites are distributed over a large surface of the protein, it appears that the molecule may interact with several regions of 16S rRNA.

PMID: 8251502 [PubMed - indexed for MEDLINE]



Source: PubMed
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