Beta-lactamase inhibitor protein
| BLIP | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of tem-1 beta-lactamase / beta-lactamase inhibitor protein complex | |||||||||
| Identifiers | |||||||||
| Symbol | BLIP | ||||||||
| Pfam | PF07467 | ||||||||
| Pfam clan | CL0320 | ||||||||
| InterPro | IPR009099 | ||||||||
| SCOP2 | 1s0w / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, the beta-lactamase-inhibitor proteins (BLIP) 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 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.[1] BLIP shows no sequence similarity with BLIP-II, even though both bind to and inhibit TEM-1.[2]
References
- ^ Strynadka NC, Jensen SE, Alzari PM, James MN (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): 290â7. PMID 8605632.
{{cite journal}}: C1 control character in|pages=at position 5 (help); Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ Lim D, Park HU, De Castro L, Kang SG, Lee HS, Jensen S, Lee KJ, Strynadka NC (2001). "Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase". Nat. Struct. Biol. 8 (10): 848â52. doi:10.1038/nsb1001-848. PMID 11573088.
{{cite journal}}: C1 control character in|pages=at position 5 (help); Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link)
