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首页> 外文期刊>Journal of Molecular Biology >Target-induced conformational adaptation of calmodulin revealed by the crystal structure of a complex with nematode Ca2+/calmodulin-dependent kinase kinase peptide
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Target-induced conformational adaptation of calmodulin revealed by the crystal structure of a complex with nematode Ca2+/calmodulin-dependent kinase kinase peptide

机译：线虫Ca2 + /钙调蛋白依赖性激酶激酶肽复合物的晶体结构揭示钙调蛋白的靶标诱导构象适应性

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摘要

Calmodulin (CaM) is a ubiquitous calcium (Ca2+) sensor which binds and regulates protein serine/threonine kinases along with many other proteins in a Ca2+-dependent manner. For thus multi-functionality, conformational plasticity is essential; however, the nature and magnitude of CaM's plasticity still remains largely undetermined. Here, we present the 1.8 Angstrom resolution crystal structure of Ca2+/CaM, complexed with the 27-residue synthetic peptide corresponding to the CaM-binding domain of the nematode Caenorhabditis elegans Ca2+/CaM-dependent kinase kinase (CaMKK). The peptide bound in this crystal structure is a homologue of the previously NMR-derived complex with rat CaMKK, but benefits from improved structural resolution. Careful comparison of the present structure to previous crystal structures of CaM complexed with unrelated peptides derived from myosin light chain kinase and CaM kinase II, allow a quantitative analysis of the differences in the relative orientation of the N and C-terminal domains of CaM, defined as a screw axis rotation angle ranging from 156 degrees to 196 degrees. The principal differences in CaM interaction with various peptides are associated with the N-terminal domain of CaM. Unlike the C-terminal domain, which remains unchanged internally, the N-terminal domain of CaM displays significant differences in the EF-hand helix orientation between this and other CaM structures. Three hydrogen bonds between CaM and the peptide (E87-R336, E87-T339 and K75-T339) along with two salt bridges (E11-R349 and E114-K334) are the most probable determinants for the binding direction of the CaMKK peptide to CaM.
机译：钙调蛋白（CaM）是一种普遍存在的钙（Ca2 +）传感器，它以依赖Ca2 +的方式结合并调节蛋白质丝氨酸/苏氨酸激酶以及许多其他蛋白质。对于这样的多功能性，构象可塑性是必不可少的。但是，CaM可塑性的性质和大小仍未确定。在这里，我们介绍了Ca2 + / CaM的1.8埃分辨率晶体结构，与对应于线虫秀丽隐杆线虫Ca2 + / CaM依赖性激酶激酶（CaMKK）的CaM结合域的27个残基合成肽复合。结合在该晶体结构中的肽是先前NMR衍生的与大鼠CaMKK的复合物的同源物，但得益于改进的结构分辨率。仔细比较目前的结构与CaM与肌球蛋白轻链激酶和CaM激酶II衍生的无关肽复合的先前晶体结构，可以定量分析CaM N和C末端结构域相对方向的差异，定义如下作为丝杠轴的旋转角度，范围从156度到196度。 CaM与各种肽相互作用的主要差异与CaM的N端结构域有关。与内部保持不变的C末端结构域不同，CaM的N末端结构域在此和其他CaM结构之间的EF手螺旋方向上显示出显着差异。 CaM和肽（E87-R336，E87-T339和K75-T339）之间的三个氢键以及两个盐桥（E11-R349和E114-K334）是CaMKK肽与CaM结合方向的最可能决定因素。

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