Beta-lactamase inhibitor protein explained

Symbol:	BLIP
Beta-Lactamase Inhibitor Protein
Width:	180px
Pfam:	PF07467
Pfam Clan:	CL0320
Interpro:	IPR009099
Scop:	1s0w

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]

Notes and References

1. Strynadka NC, Jensen SE, Alzari PM, James MN . 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 . March 1996 . 8605632 . 10.1038/nsb0396-290. 22870717 .
2. Lim D, Park HU, De Castro L, Kang SG, Lee HS, Jensen S, Lee KJ, Strynadka NC . 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 . October 2001 . 11573088 . 10.1038/nsb1001-848 . 29753789 .