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首页> 外文期刊>Journal of structural and functional genomics >Structural basis of CoA recognition by the Pyrococcus single-domain CoA-binding proteins
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Structural basis of CoA recognition by the Pyrococcus single-domain CoA-binding proteins

机译：球菌单结构域CoA结合蛋白识别CoA的结构基础

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The single-domain coenzyme A (CoA)-binding protein is conserved in bacteria, archaea, and a few eukaryal taxa. It consists of a Rossmann-fold domain, belonging to the FAD/NAD(P)-binding `superfamily. The crystal structure of the Thermus thermophilus single-domain CoA-binding protein, TTHA1899, has been determined and it has been demonstrated, by isothermal titration calorimetry, that the protein interacts with CoA [Wada T. et?al. Acta Crystallogr D Biol Crystallogr 59 (2003) 1213]. In the present study, we determined the crystal structures of an orthologous protein from the archaeon Pyrococcus horikoshii (PH1109), alone and complexed with CoA, at 1.65?? and 1.70?? resolutions, respectively, and that of P. furiosus protein (PF0725) in the CoA-bound form at 1.70??. The CoA-bound structures are very similar to each other, revealing that the Pyrococcus proteins bind CoA in a 1:1 stoichiometry. Five loop-containing regions form the CoA-binding groove, to which the CoA molecule is docked. A comparison of the structures and the sequences of the Pyrococcus proteins with those of the T. theromphilus orthologue TTHA1899 indicated that archaeal and bacterial single-domain CoA-binding proteins share the same CoA-binding mode. Nevertheless, many of the peripheral residues involved in the hydrogen-bonding/electrostatic interactions with CoA are not strictly conserved in the family. The CoA interaction of the single-domain CoA-binding proteins is significantly different and much more extensive than that of the multi-subunit/multi-domain CoA-binding protein succinyl-CoA synthetase.
机译：单域辅酶A（CoA）结合蛋白在细菌，古细菌和一些真核生物类群中是保守的。它由Rossmann折叠域组成，属于FAD / NAD（P）结合`超家族。已经确定了嗜热栖热菌单结构域CoA结合蛋白TTHA1899的晶体结构，并通过等温滴定量热法证明了该蛋白与CoA相互作用[Wada T. et al。，J.Am.Chem.Soc。，2005，8，1959]。晶体学报D Biol Crystallogr 59（2003）1213]。在本研究中，我们确定了古and热球菌（PH1109）的直系同源蛋白质的晶体结构，该蛋白质单独并与CoA配合，在1.65？和1.70 ？？分辨率分别为CoA-结合形式的狂犬热疫病菌蛋白（PF0725）在1.70 ??。结合CoA的结构彼此非常相似，表明火球菌蛋白质以1：1的化学计量比结合CoA。五个包含环的区域形成CoA结合凹槽，CoA分子停靠在该凹槽中。嗜热链球菌蛋白与嗜热链球菌TTHA1899的结构和序列的比较表明，古细菌和细菌单结构域CoA结合蛋白共享相同的CoA结合模式。尽管如此，该家族中并不严格保留与CoA进行氢键键合/静电相互作用的许多周边残基。单域CoA结合蛋白的CoA相互作用显着不同，并且比多亚基/多域CoA结合蛋白琥珀酰CoA合成酶的CoA相互作用更广泛。

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