1jtd

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spinqualitylabelsall models 1jtd, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase

Overview

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.

About this Structure

1JTD is a Protein complex structure of sequences from Escherichia coli and Streptomyces exfoliatus with CA as ligand. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.

Reference

Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase., Lim D, Park HU, De Castro L, Kang SG, Lee HS, Jensen S, Lee KJ, Strynadka NC, Nat Struct Biol. 2001 Oct;8(10):848-52. PMID:11573088

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