Crystal structure and kinetic analysis of β-lactamase inhibitor protein-II in complex with TEM-1 β-lactamase
Crystal structure and kinetic analysis of β-lactamase inhibitor protein-II in complex with TEM-1 β-lactamase
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DOI：
10.1038/nsb1001-848
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发表时间：
2001-10-01
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影响因子：
--
通讯作者：
Strynadka, NCJ
中科院分区：
文献类型：
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作者：
Lim, D;Park, HU;Strynadka, NCJ
与 TEM-1 β-内酰胺酶复合的 28 kDa β-内酰胺酶抑制剂蛋白-II (BLIP-II) 的结构已确定为 2.3 埃分辨率。 BLIP-II 是由土壤细菌脱叶链霉菌 SMF19 产生的分泌蛋白，能够以亚纳摩尔亲和力结合并抑制 TEM-1。 BLIP-II 是一种七叶 β 螺旋桨，具有独特的叶片图案，仅由三个反平行 β 链组成。整体折叠与人类染色体浓缩调节因子（RCC1）的核心结构高度相似。尽管 BLIP-II 与第一个有结构数据的 β-内酰胺酶抑制剂蛋白 BLIP 不具有相同的折叠，但两种复合物的比较揭示了许多相似之处，并提供了对 TEM-1-BLIP 和 TEM-1-BLIP-II 界面的关键组成部分的进一步见解。我们的基因敲除研究和扫描电子显微镜的初步结果也揭示了 BLIP-II 在孢子形成中的关键作用。
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 Angstrom 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.