1JTD
Crystal structure of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase
1JTD の概要
エントリーDOI | 10.2210/pdb1jtd/pdb |
分子名称 | TEM-1 beta-lactamase, beta-lactamase inhibitor protein II, CALCIUM ION, ... (4 entities in total) |
機能のキーワード | protein-protein complex, tem-1 beta-lactamase, beta-lactamase inhibitor protein-ii, blip-ii, hydrolase-inhibitor complex, hydrolase/inhibitor |
由来する生物種 | Escherichia coli 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 56527.41 |
構造登録者 | Lim, D.C.,Park, H.U.,De Castro, L.,Kang, S.G.,Lee, H.S.,Jensen, S.,Lee, K.J.,Strynadka, N.C.J. (登録日: 2001-08-20, 公開日: 2001-10-03, 最終更新日: 2024-10-30) |
主引用文献 | Lim, D.,Park, H.U.,De Castro, L.,Kang, S.G.,Lee, H.S.,Jensen, S.,Lee, K.J.,Strynadka, N.C. Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase. Nat.Struct.Biol., 8:848-852, 2001 Cited by PubMed Abstract: 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. PubMed: 11573088DOI: 10.1038/nsb1001-848 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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