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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases.
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Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases.

机译：与可溶性鸟苷酸环化酶有关的与氧结合的血红素结构域的晶体结构。

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摘要

Soluble guanylate cyclases are nitric oxide-responsive signaling proteins in which the nitric oxide sensor is a heme-binding domain of unknown structure that we have termed the heme-NO and oxygen binding (H-NOX) domain. H-NOX domains are also found in bacteria, either as isolated domains, or are fused through a membrane-spanning region to methyl-accepting chemotaxis proteins. We have determined the crystal structure of an oxygen-binding H-NOX domain of one such signaling protein from the obligate anaerobe Thermoanaerobacter tengcongensis at 1.77-angstroms resolution, revealing a protein fold unrelated to known structures. Particularly striking is the structure of the protoporphyrin IX group, which is distorted from planarity to an extent not seen before in protein-bound heme groups. Comparison of the structure of the H-NOX domain in two different crystal forms suggests a mechanism whereby alteration in the degree of distortion of the heme group is coupled to changes on the molecular surface of the H-NOX domain and potentially to changes in intermolecular interactions.
机译：可溶性鸟苷酸环化酶是一氧化氮响应信号蛋白，其中一氧化氮传感器是结构未知的血红素结合域，我们称其为血红素-NO和氧结合（H-NOX）域。 H-NOX结构域也可以在细菌中发现，可以是分离的结构域，也可以通过跨膜区域与甲基化趋化蛋白融合。我们已经确定了一种信号信号蛋白的氧结合H-NOX结构域的晶体结构，该信号蛋白来自专心的厌氧嗜热气单胞菌腾克丛，分辨率为1.77埃，揭示了与已知结构无关的蛋白质折叠。尤其令人惊奇的是原卟啉IX基团的结构从平面性变形到在蛋白质结合的血红素基团中前所未有的程度。比较两种不同晶体形式的H-NOX结构域的结构表明了一种机制，其中血红素基团畸变程度的变化与H-NOX结构域分子表面的变化以及分子间相互作用的变化相关。

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