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The structure of a novel membrane‐associated 6‐phosphogluconate dehydrogenase from Gluconacetobacter diazotrophicus (Gd6PGD) reveals a subfamily of short‐chain 6PGDs
The FEBS Journal ( IF 5.5 ) Pub Date : 2020-07-04 , DOI: 10.1111/febs.15472
Pedro D Sarmiento-Pavía 1 , Annia Rodríguez-Hernández 2 , Adela Rodríguez-Romero 2 , Martha E Sosa-Torres 1
Affiliation  

The enzyme 6‐phosphogluconate dehydrogenase catalyzes the conversion of 6‐phosphogluconate to ribulose‐5‐phosphate. It represents an important reaction in the oxidative pentose phosphate pathway, producing a ribose precursor essential for nucleotide and nucleic acid synthesis. We succeeded, for the first time, to determine the three‐dimensional structure of this enzyme from an acetic acid bacterium, Gluconacetobacter diazotrophicus (Gd6PGD). Active Gd6PGD, a homodimer (70 kDa), was present in both the soluble and the membrane fractions of the nitrogen‐fixing microorganism. The Gd6PGD belongs to the newly described subfamily of short‐chain (333 AA) 6PGDs, compared to the long‐chain subfamily (480 AA; e.g., Ovis aries, Homo sapiens). The shorter amino acid sequence in Gd6PGD induces the exposition of hydrophobic residues in the C‐terminal domain. This distinct structural feature is key for the protein to associate with the membrane. Furthermore, in terms of function, the short‐chain 6PGD seems to prefer NAD+ over NADP+, delivering NADH to the membrane‐bound NADH dehydrogenase of the microorganisms required by the terminal oxidases to reduce dioxygen to water for energy conservation.

中文翻译:

重氮糖杆菌属(Gd6PGD)的新型膜相关6-磷酸葡萄糖脱氢酶的结构揭示了短链6PGD的一个亚家族

6-磷酸葡萄糖酸脱氢酶催化6-磷酸葡萄糖酸转化为5-5核糖。它代表了氧化戊糖磷酸途径中的重要反应,产生了核苷酸和核酸合成必不可少的核糖前体。我们首次成功地从醋酸细菌重氮糖杆菌(Gd 6PGD)中确定了该酶的三维结构。固氮微生物的可溶性和膜级分中均存在活性Gd 6PGD,即同型二聚体(70 kDa)。所述的Gd 6PGD属于短链(333 AA)6PGDs新描述的亚家族,相比于长链亚科(480 AA;例如,Ovis aries,智人)。Gd 6PGD中较短的氨基酸序列可诱导C末端结构域中疏水残基的暴露。这种独特的结构特征是蛋白质与膜结合的关键。此外,就功能而言,短链6PGD似乎更喜欢NAD +而不是NADP +,将NADH传递至末端氧化酶所需的微生物的膜结合NADH脱氢酶,以将双氧还原为水以节约能源。
更新日期:2020-07-04
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