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首页> 外文期刊>Acta crystallographica. Section D, Structural biology >Intermediates in allosteric equilibria of DnaK-ATP interactions with substrate peptides
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Intermediates in allosteric equilibria of DnaK-ATP interactions with substrate peptides

机译：中间体DnaK-ATP的变构平衡与底物肽的相互作用

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摘要

Hsp70 molecular chaperones facilitate protein disaggregation and proper folding through iterative cycles of polypeptide binding and release that are allosterically coupled to ATP binding and hydrolysis. Hsp70s are ubiquitous and highly conserved across all of life; they bind ATP at an N-terminal nucleotide-binding domain (NBD) and client peptides in the substrate-binding domain (SBD). The NBD and SBD are connected by a highly conserved linker segment that is integrated into the NBD when ATP is bound but is flexible when the NBD is nucleotide-free or bound with ADP Allosteric coupling is lost when the linker is flexible, and the freed SBD binds peptide clients with high affinity. It was recently discovered that Hsp70-ATP is in an equilibrium between a restraining state (R) with little affinity for peptides and a low ATPase activity, and a stimulating state (S) that binds peptides efficiently, but with rapid kinetics, and has a relatively high ATPase activity. While attempting to characterize the S state, crystal structures of DnaK-ATP were obtained that demonstrate intrinsic Hsp70 plasticity that affects binding interactions with substrate peptides. These structures provide insights into intermediate states along transition pathways in the Hsp70 chaperone cycle.
机译：Hsp70陪伴促进蛋白质分子解集和适当的折叠多肽的绑定和迭代周期变构耦合ATP释放绑定和水解。高度保守的在所有的生活;ATP的氨基端nucleotide-binding域(NBD)和客户端肽substrate-binding域(作为)。连接由一个高度保守的链接吗段时融入NBD ATP绑定但NBD时灵活吗和ADP变构nucleotide-free或绑定耦合是失去了灵活的连接器时,作为结合肽释放客户提供高亲和力。Hsp70-ATP之间的一个平衡抑制状态(R)与亲和力肽和atp酶活性较低,结合肽刺激状态(年代)有效,但快速动力学,相对较高的atp酶活性。描述S状态,晶体结构DnaK-ATP获得证明内在Hsp70可塑性影响绑定与底物肽的相互作用。结构提供见解的中间体州过渡Hsp70的途径女伴周期。

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