Beta-lactamase inhibitor protein

Beta-Lactamase Inhibitor Proteins (BLIPs) are a family of proteins produced by bacterial species including Streptomyces. BLIP acts as a potent inhibitor of beta-lactamases such as TEM-1, which is the most widespread resistance enzyme to penicillin antibiotics. BLIP binds competitively the surface of TEM-1 and inserting residues into the active site to make direct contacts with catalytic residues. BLIP is able to inhibit a variety of class A beta-lactamases, possibly through flexibility of its two domains. The two tandemly repeated domains of BLIP have an α2-β4 structure, the β-hairpin loop from domain 1 inserting into the active site of beta-lactamase.[1] BLIP shows no sequence similarity with BLIP-II, even though both bind to and inhibit TEM-1.[2]

Beta-lactamase Inhibitory Protein (white) complexed with beta-lactamase (grey) with key interaction residues highlighted (red). (PDB: 3C7V​)
Beta-Lactamase Inhibitor Protein
Beta-Lactamase Inhibitory Protein (BLIP) with α-helices in red, β-sheets in blue, disulphides in yellow. (PDB: 3C7V​)
Identifiers
SymbolBLIP
PfamPF07467
Pfam clanCL0320
InterProIPR009099
SCOP21s0w / SCOPe / SUPFAM

References
  1. Strynadka NC, Jensen SE, Alzari PM, James MN (March 1996). "A potent new mode of beta-lactamase inhibition revealed by the 1.7 A X-ray crystallographic structure of the TEM-1-BLIP complex". Nat. Struct. Biol. 3 (3): 290–7. doi:10.1038/nsb0396-290. PMID 8605632. S2CID 22870717.
  2. Lim D, Park HU, De Castro L, Kang SG, Lee HS, Jensen S, Lee KJ, Strynadka NC (October 2001). "Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase". Nat. Struct. Biol. 8 (10): 848–52. doi:10.1038/nsb1001-848. PMID 11573088. S2CID 29753789.
This article incorporates text from the public domain Pfam and InterPro: IPR009099
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