1EY1
SOLUTION STRUCTURE OF ESCHERICHIA COLI NUSB
Summary for 1EY1
| Entry DOI | 10.2210/pdb1ey1/pdb |
| Descriptor | ANTITERMINATION FACTOR NUSB (1 entity in total) |
| Functional Keywords | transcirption termination, transcription |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 15710.03 |
| Authors | Altieri, A.S.,Mazzulla, M.J.,Horita, D.A.,Coats, R.H.,Wingfield, P.T.,Byrd, R.A. (deposition date: 2000-05-05, release date: 2000-06-14, Last modification date: 2024-05-22) |
| Primary citation | Altieri, A.S.,Mazzulla, M.J.,Horita, D.A.,Coats, R.H.,Wingfield, P.T.,Das, A.,Court, D.L.,Byrd, R.A. The structure of the transcriptional antiterminator NusB from Escherichia coli. Nat.Struct.Biol., 7:470-474, 2000 Cited by PubMed Abstract: 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. PubMed: 10881193DOI: 10.1038/75869 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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