Crystal structure of the Bacillus stearothermophilus anti-sigma factor SpoIIAB with the sporulation sigma factor sigmaF.
Crystal structure of the Bacillus stearothermophilus anti-sigma factor SpoIIAB with the sporulation sigma factor sigmaF.
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DOI：
10.2210/pdb1l0o/pdb
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发表时间：
2002-03
期刊：
影响因子：
64.5
通讯作者：
E. Campbell;S. Masuda;Jing L. Sun;Oriana Muzzin;C. Olson;Sheng Wang;S. Darst
中科院分区：
文献类型：
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作者：
E. Campbell;S. Masuda;Jing L. Sun;Oriana Muzzin;C. Olson;Sheng Wang;S. Darst
芽孢杆菌产孢过程中细胞类型特异性转录是由sigmaF建立的。SpoIIAB是一种结合并负调控sigmaF的抗sigma蛋白，也是一种磷酸化并失活抗sigma蛋白SpoIIAA的丝氨酸激酶。在2.9 A的分辨率下，sigmaF以低亲和力的ADP形式与spoiab二聚体结合。spoiab采用atp酶和组氨酸激酶的GHKL超家族折叠。sigmaF结构域与两个SpoIIAB单体接触，而80%的sigma因子是无序的。这种相互作用阻断了sigmaF的RNA聚合酶结合表面，解释了SpoIIAB抗sigma活性。该结构还解释了SpoIIAB对其靶sigma因子的特异性，并结合遗传和生化数据，为SpoIIAA抗-抗sigma活性的机制提供了新的见解。
Cell type-specific transcription during Bacillus sporulation is established by sigmaF. SpoIIAB is an anti-sigma that binds and negatively regulates sigmaF, as well as a serine kinase that phosphorylates and inactivates the anti-anti-sigma SpoIIAA. The crystal structure of sigmaF bound to the SpoIIAB dimer in the low-affinity, ADP form has been determined at 2.9 A resolution. SpoIIAB adopts the GHKL superfamily fold of ATPases and histidine kinases. A domain of sigmaF contacts both SpoIIAB monomers, while 80% of the sigma factor is disordered. The interaction occludes an RNA polymerase binding surface of sigmaF, explaining the SpoIIAB anti-sigma activity. The structure also explains the specificity of SpoIIAB for its target sigma factors and, in combination with genetic and biochemical data, provides insight into the mechanism of SpoIIAA anti-anti-sigma activity.