Beta-lactamase-inhibitor protein BLIP, structural domain <p>The beta-lactamase-inhibitor protein (BLIP) is produced by Streptomyces species. 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 to TEM-1 and makes direct contacts with TEM-1 active site 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 alpha(2)-beta(4) structure, the beta-hairpin loop from domain 1 inserting into the active site of beta-lactamase [<cite idref="PUB00013170"/>]. BLIP shows no sequence similarity with BLIP-II, even though both bind to and inhibit TEM-1 [<cite idref="PUB00013255"/>].</p>This entry represents the structural domains of BLIP [<cite idref="PUB00040912"/>].