The structure of the transcriptional antiterminator NusB from Escherichia coli
| Autor: | Donald L. Court, Marie J. Mazzulla, R.A. Byrd, Amanda S. Altieri, Paul T. Wingfield, David A. Horita, R.H. Coats, Asis Das |
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| Rok vydání: | 2000 |
| Předmět: |
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Molecular Molecular Sequence Data Sequence alignment Biology Crystallography X-Ray medicine.disease_cause Biochemistry Protein Structure Secondary Article Conserved sequence Protein structure Bacterial Proteins Structural Biology Escherichia coli Genetics medicine Amino Acid Sequence Binding site Nuclear Magnetic Resonance Biomolecular Peptide sequence Conserved Sequence Binding Sites Escherichia coli Proteins RNA-Binding Proteins RNA Mycobacterium tuberculosis Solutions Transcription antitermination Mutation Sequence Alignment Protein Binding Transcription Factors |
| Zdroj: | Nat Struct Biol |
| ISSN: | 1072-8368 |
| DOI: | 10.1038/75869 |
| Popis: | We have determined the solution structure of NusB, a transcription antitermination protein from Escherichia coli. The structure reveals a novel, all alpha-helical protein fold. NusB mutations that cause a loss of function (NusB5) or alter specificity for RNA targets (NusB101) are localized to surface residues and likely affect RNA-protein or protein-protein interactions. Residues that are highly conserved among homologs stabilize the protein core. The solution structure of E. coli NusB presented here resembles that of Mycobacterium tuberculosis NusB determined by X-ray diffraction, but differs substantially from a solution structure of E. coli NusB reported earlier. |
| Databáze: | OpenAIRE |
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