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- PDB-1rip: RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE THREE-DIMENSIONAL ... -

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Entry
Database: PDB / ID: 1rip
TitleRIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE THREE-DIMENSIONAL STRUCTURE BY 1H-AND 15N-NMR
ComponentsRIBOSOMAL PROTEIN S17
KeywordsRIBOSOMAL PROTEIN
Function / homology
Function and homology information


cytosolic small ribosomal subunit / rRNA binding / structural constituent of ribosome / translation
Similarity search - Function
Nucleic acid-binding proteins / 30S ribosomal protein S17 / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Ribosomal protein S17, conserved site / Ribosomal protein S17 signature. / Ribosomal protein S17/S11 / Ribosomal protein S17 / Nucleic acid-binding, OB-fold / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Small ribosomal subunit protein uS17
Similarity search - Component
Biological speciesGeobacillus stearothermophilus (bacteria)
MethodSOLUTION NMR
AuthorsGolden, B.L. / Hoffman, D.W. / Ramakrishnan, V. / White, S.W.
Citation
Journal: Biochemistry / Year: 1993
Title: Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.
Authors: Golden, B.L. / Hoffman, D.W. / Ramakrishnan, V. / White, S.W.
#1: Journal: Mol.Gen.Genet. / Year: 1979
Title: A Missense Mutation in the Gene Coding for Ribosomal Protein S17 (Rpsq) Leading to Ribosomal Assembly Defectivity in Escherichia Coli
Authors: Herzog, A. / Yaguchi, M. / Cabezon, T. / Corchuelo, M.-C. / Petre, J. / Bollen, A.
#2: Journal: J.Mol.Biol. / Year: 1976
Title: Alteration of Ribosomal Protein S17 by Mutation Linked to Neamine Resistance in Escherichia Coli. II. Localization of the Amino Acid Replacement in Protein S17 from a Neaa Mutant
Authors: Yaguchi, M. / Wittmann, H.G. / Cabezon, T. / Dewilde, M. / Villarroel, R. / Herzog, A. / Bollen, A.
History
DepositionAug 17, 1993Processing site: BNL
Revision 1.0Oct 31, 1993Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: RIBOSOMAL PROTEIN S17


Theoretical massNumber of molelcules
Total (without water)9,5551
Polymers9,5551
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: THERE IS A ONE RESIDUE BETA-BULGE IN THE FIFTH STRAND. RESIDUES 77 AND 78 OCCUPY THE SITE OF A SINGLE RESIDUE IN A REGULAR STRAND.
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)6 / -
Representative

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Components

#1: Protein RIBOSOMAL PROTEIN S17


Mass: 9555.309 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Geobacillus stearothermophilus (bacteria)
References: UniProt: P23828

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR ensembleConformers submitted total number: 6

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