Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase.
The structure of the 28 kDa beta-lactamase inhibitor protein-II (BLIP-II) in complex with the TEM-1 beta-lactamase has been determined to 2.3 A resolution. BLIP-II is a secreted protein produced by the soil bacterium Streptomyces exfoliatus SMF19 and is able to bind and inhibit TEM-1 with subnanomolar affinity. BLIP-II is a seven-bladed beta-propeller with a unique blade motif consisting of only three antiparallel beta-strands. The overall fold is highly similar to the core structure of the human regulator of chromosome condensation (RCC1). Although BLIP-II does not share the same fold with BLIP, the first beta-lactamase inhibitor protein for which structural data was available, a comparison of the two complexes reveals a number of similarities and provides further insights into key components of the TEM-1-BLIP and TEM-1-BLIP-II interfaces. Our preliminary results from gene knock-out studies and scanning electron microscopy also reveal a critical role of BLIP-II in sporulation.
Lim
D
D
Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, Canada.
Park
H U
HU
De Castro
L
L
Kang
S G
SG
Lee
H S
HS
Jensen
S
S
Lee
K J
KJ
Strynadka
N C
NC
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008855:Microscopy, Electron, Scanning; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013302:Streptomyces / Q000737:chemistry* / Q000648:ultrastructure; D001618:beta-Lactamases / Q000737:chemistry*
D001426:Bacterial Proteins; D008024:Ligands; C065596:beta-lactamase-inhibitor protein, Streptomyces; D001618:beta-Lactamases; C034413:beta-lactamase TEM-1