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Barstar

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Barstar (barnase inhibitor)
The tightly bound complex between barstar and barnase, the ribonuclease barstar inhibits. Barstar is colored by secondary structure and barnase is colored in blue.[1]
Identifiers
SymbolBarstar
PfamPF01337
InterProIPR000468
SCOP21brs / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1b2sD:2-89 1bgsG:2-89 1x1wD:2-89

1x1xD:2-89 1brsD:2-89 1b27F:2-89 1bta :2-89 1ab7 :2-89 1b3sE:2-89 1b2uF:2-89 1x1yE:2-89 1x1uE:2-89 1ay7B:2-89 1a19B:2-89 1btb :2-89

1l1kA:2-20

Barstar is a small protein synthesized by the bacterium Bacillus amyloliquefaciens. Its function is to inhibit the ribonuclease activity of its binding partner barnase, with which it forms an extraordinarily tightly bound complex within the cell until barnase is secreted.[2][3] Expression of barstar is necessary to counter the lethal effect of expressed active barnase. The structure of the barnase-barstar complex is known.[4]

References

  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): 8878–89. doi:10.1021/bi00196a004. PMID 8043575.
  2. ^ Hartley RW (1989). "Barnase and barstar: two small proteins to fold and fit together". Trends Biochem. Sci. 14 (11): 450–454. doi:10.1016/0968-0004(89)90104-7. PMID 2696173.
  3. ^ Hartley RW (1988). "Barnase and barstar. Expression of its cloned inhibitor permits expression of a cloned ribonuclease". J. Mol. Biol. 202 (4): 913–915. doi:10.1016/0022-2836(88)90568-2. PMID 3050134.
  4. ^ Fersht AR, Buckle AM, Schreiber G (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.
This article incorporates text from the public domain Pfam and InterPro: IPR000468


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