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Crystal structure of chaperonin-60 from Paracoccus denitrificans

机译：反硝化链球菌伴侣蛋白60的晶体结构

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摘要

The crystal structure of chaperonin-60 from Paracoccus denitrificans (P.cpn60) has been determined at 3.2 Angstrom resolution by the molecular replacement method. Two heptameric rings of identical subunits of P.cpn60 in adjacent asymmetric units are stacked in a back-to-back manner and form a cylinder, as found in GroEL, cpn60 from Escherichia coli. With respect to the unliganded GroEL structure, each subunit of P.cpn60 tilts 2 degrees outwards and the apical domain twists 4 degrees counter-clockwise in the top view in a hinge-like manner, rendering the central hole 5 Angstrom wider. Despite the sub-ardt tilts, both rings in P.cpn60 contact at two sites of the equatorial domain in the same way as in GroEL. Interactions between residues 434 and 434, and 463 and 463 observed in GroEL were not found in P.cpn60, and the interaction between 452 and 461 was weaker in P.cpn60 than in GroEL. The unique hydrogen bond between 468 and 471 was observed at the right site in P.cpn60, which could account for why the subunits tilt outwards. The contact surface area was reduced at the left site, which is similar to the observed changes in the GroEL structures induced by ATP binding. In general, inter-ring interactions in P.cpn60 were weakened, which is consistent with findings that P.cpn60 is observed in single-ring forms as well as in double-ring forms.
机译：脱氮副球菌伴侣蛋白60（P.cpn60）的晶体结构已通过分子置换方法在3.2埃分辨率下确定。 P.cpn60的相同亚基在相邻的不对称单元中的两个七聚环以背对背的方式堆叠，并形成圆柱体，如在GroEL中发现的来自大肠杆菌的cpn60。对于未配位的GroEL结构，P.cpn60的每个亚基在俯视图中以铰链状向外倾斜2度，顶端区域逆时针扭曲4度，使中心孔变宽5埃。尽管亚ardt倾斜，P.cpn60中的两个环都以与GroEL中相同的方式在赤道域的两个位置接触。在GroeEL中观察到的残基434和434之间以及463和463之间的相互作用在P.cpn60中没有发现，而P.cpn60中的452和461之间的相互作用比GroEL中的弱。在P.cpn60的正确位置观察到468和471之间的独特氢键，这可以解释亚基为何向外倾斜的原因。接触表面积在左侧部位减少，这类似于由ATP结合诱导的GroEL结构的观察到的变化。通常，P.cpn60中的环间相互作用会减弱，这与发现单环形式和双环形式的P.cpn60一致。

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