Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The structure of the transcriptional antiterminator NusB from Escherichia coli.,Altieri AS, Mazzulla MJ, Horita DA, Coats RH, Wingfield PT, Das A, Court DL, Byrd RA Nat Struct Biol. 2000 Jun;7(6):470-4. PMID:10881193[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Altieri AS, Mazzulla MJ, Horita DA, Coats RH, Wingfield PT, Das A, Court DL, Byrd RA. The structure of the transcriptional antiterminator NusB from Escherichia coli. Nat Struct Biol. 2000 Jun;7(6):470-4. PMID:10881193 doi:10.1038/75869
