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首页> 外文期刊>Biochemistry >Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling.
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Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling.

机译：甲烷单加氧酶通过异核NMR和分子建模得到的组分B的溶液结构。

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Methane monooxygenase (MMO) is a nonheme iron-containing enzyme which consists of three protein components: a hydroxylase (MMOH), an NADH-linked reductase (MMOR), and a small "B" component (MMOB) which plays a regulatory role. Here, 1H, 13C, 15N heteronuclear 2D and 3D NMR spectroscopy has been used to derive the solution structure of the 138 amino acid MMOB protein in the monomer state. Pulse field gradient NMR self-diffusion measurements indicate predominant formation of dimers at 1 mM MMOB and monomers at or below 0.2 mM. MMOB is active as a monomer. Aggregate exchange broadening and limited solubility dictated that multidimensional heteronuclear NMR experiments had to be performed at a protein concentration of 0.2 mM. Using 1340 experimental constraints (1182 NOEs, 98 dihedrals, and 60 hydrogen bonding) within the well-folded part of the protein (residues 36-126), MMOB structural modeling produced a well-defined, compact alpha/beta fold which consists of three alpha-helices and six antiparallel beta-strands arranged in two domains: a betaalphabetabeta and a betaalphaalphabetabeta. Excluding the ill-defined N- and C-terminal segments (residues 1-35 and 127-138), RMS deviations are 1.1 A for backbone atoms and 1.6 A for all non-hydrogen atoms. Compared to the lower resolution NMR structure for the homologous protein P2 from the Pseudomonas sp. CF600 phenol hydroxylase system (RMSD = 2.48 A for backbone atoms) (Qian, H., Edlund, U., Powlowski, J., Shingler, V., and Sethson, I. (1997) Biochemistry, 36, 495-504), that of MMOB reveals a considerably more compact protein. In particular, MMOB lacks the large "doughnut" shaped cavity reported for the P2 protein. This difference may result from the limited number of long-range NOEs that were available for use in the modeling of the P2 structure. This NMR-derived structure of MMOB, therefore, presents the first high-resolution structure of a small protein effector of a nonheme oxygenase system.
机译：甲烷单加氧酶（MMO）是一种非血红素铁酶，它由三个蛋白质成分组成：羟化酶（MMOH），NADH连接的还原酶（MMOR）和小的“ B”成分（MMOB），起着调节作用。此处，已使用1H，13C，15N异核2D和3D NMR光谱法得出了单体状态下138个氨基酸的MMOB蛋白的溶液结构。脉冲场梯度NMR自扩散测量表明，在1 mM MMOB处主要形成二聚体，在0.2 mM或以下处主要形成单体。 MMOB作为单体具有活性。聚集交换加宽和有限的溶解度决定必须在0.2 mM的蛋白质浓度下进行多维异核NMR实验。在蛋白质折叠良好的部分（残基36-126）中使用1340个实验约束（1182个NOE，98个二面体和60个氢键），MMOB结构建模产生了定义明确的紧凑α/β折叠，该折叠由三个alpha螺旋和六个反平行的beta链排列在两个域中：betaalphabetabeta和betaalphaalphabetabeta。排除不确定的N和C末端链段（残基1-35和127-138），RMS偏差对于主链原子为1.1 A，对于所有非氢原子为1.6A。与来自假单胞菌属物种的同源蛋白P2的较低分辨率NMR结构相比。 CF600酚羟化酶系统（骨架原子的RMSD = 2.48 A）（Qian，H.，Edlund，U.，Powlowski，J.，Shingler，V.，and Sethson，I.（1997）Biochemistry，36，495-504） ，MMOB的蛋白质显示了相当紧凑的蛋白质。特别是，MMOB缺少针对P2蛋白报道的大的“甜甜圈”形空腔。这种差异可能是由于可用于P2结构建模的远程NOE数量有限而导致的。因此，MMOB的这种NMR衍生结构提供了非血红素加氧酶系统的小蛋白效应子的第一个高分辨率结构。

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