The tightly bound complex between barnase and its inhibitor barstar. Barnase is colored by secondary structure and barstar is colored in blue.[1]
Identifiers
Symbol
Barnase
PDB
1BRS More structures
UniProt
P00648
Other data
EC number
3.1.27.-
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Structures
Swiss-model
Domains
InterPro
Barnase (a portmanteau of "BActerial" "RiboNucleASE") is a bacterial protein that consists of 110 amino acids and has ribonuclease activity. It is synthesized and secreted by the bacterium Bacillus amyloliquefaciens, but is lethal to the cell when expressed without its inhibitor barstar. The inhibitor binds to and occludes the ribonuclease active site, preventing barnase from damaging the cell's RNA after it has been synthesized but before it has been secreted. The barnase/barstar complex is noted for its extraordinarily tight protein-protein binding, with an on-rate of 108s−1M−1.
^PDB: 1BRS; Buckle AM, Schreiber G, Fersht AR (August 1994). "Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolution". Biochemistry. 33 (30): 8878–8889. doi:10.1021/bi00196a004. PMID 8043575.
Barnase (a portmanteau of "BActerial" "RiboNucleASE") is a bacterial protein that consists of 110 amino acids and has ribonuclease activity. It is synthesized...
activity of its binding partner barnase, with which it forms an extraordinarily tightly bound complex within the cell until barnase is secreted. Expression of...
domains, WW domain, individual domains of proteins L and G, ubiquitin, and barnase have all been studied by ϕ {\displaystyle \phi } analysis. Phi is defined...
BamHI restriction enzyme. It also synthesizes a natural antibiotic protein barnase, a widely studied ribonuclease that forms a famously tight complex with...
Bacillus amyloliquefaciens is the source of a natural antibiotic protein barnase (a ribonuclease), alpha amylase used in starch hydrolysis, the protease...
resulted in the seminal application of phi-value analysis to the study of barnase, a bacterial RNAse used in many protein folding studies. Development of...
Fersht LMB Profile Clarke, Jane (1993). Studies of disulphide mutants of barnase. jisc.ac.uk (PhD thesis). University of Cambridge. OCLC 53666398. EThOS uk...
inhibitor proteins include the barstar inhibitor of the bacterial ribonuclease barnase. Animals and plants have evolved to synthesise a vast array of poisonous...
non-natural one. To remove the former, the plasmid is inserted into cells with a barnase gene (toxic) with a premature amber codon but without the non-natural amino...
denatured RNA prior to sequencing. Similar to other ribonucleases such as barnase and RNase A, ribonuclease T1 has been popular for folding studies. Structurally...
S2CID 2130725. Vu, ND; Feng, H; Bai, Y (30 Mar 2004). "The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native...
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