| General information | | DisProt: | DP00005 | | Name: | Antitermination protein N | | Synonym(s): | REGN_LAMBD
Antitermination protein N of bacteriophage lambda
Nucleocapsid protein
Regulatory protein N
PN
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P03045 | | UniGene: | | | SwissProt: | REGN_LAMBD | | TrEMBL: | | | NCBI (GI): | 132276 | | Source organism: | Enterobacteria phage lambda (Bacteriophage lambda) | | Sequence length: | 107 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MDAQTRRRER RAEKQAQWKA ANPLLVGVSA KPVNLPILSL NRKPKSRVES ALNPIDLTVL - 60
AEYHKQIESN LQRIERKNQR TWYSKPGERG ITCSGRQKIK GKSIPLI
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| Functional narrative |
Antitermination proteins positively regulate expression of the phage early and late gene operons. Bacterial host RNA polymerase modified by these antitermination proteins transcribes through termination sites that otherwise prevent expression of the regulated genes.
N protein regulates the transition from the early to the middle stage of lytic development. It is a transcription antitermination protein that prevents termination at the rho-dependent tL and tR transcription termination sites.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 107 | | Length: | 107 | | Region sequence: |
MDAQTRRRERRAEKQAQWKAANPLLVGVSAKPVNLPILSLNRKPKSRVESALNPIDLTVL
AEYHKQIESNLQRIERKNQRTWYSKPGERGITCSGRQKIKGKSIPLI | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | | | Functional subclasses: | Protein-genomic RNA binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 5.5; d4-succinate (Aldrich) 25 mM; DTT (fresh) 2 mM; EDTA 0.2 mM; NaCl 100 mM; NaN3 0.05 mM; Varian Inova 500 MHz (spectrometer))
| References:
- Mogridge J, Legault P, Li J, Van Oene MD, Kay LE, Greenblatt J. "Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein." Mol Cell. 1998; 1(2): 265-75. PubMed: 9659923
| Comments:
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| References |
- Legault P, Li J, Mogridge J, Kay LE, Greenblatt J. "NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif." Cell. 1998; 93(2): 289-99. PubMed: 9568720
- Van Gilst MR, von Hippel PH. "Assembly of the N-dependent antitermination complex of phage lambda: NusA and RNA bind independently to different unfolded domains of the N protein." J Mol Biol. 1997; 274(2): 160-73. PubMed: 9398524
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| Comments |
AV (6-15-2010) PubMed: 9659923
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