The structure of PfGH50B, an agarase from the marine bacterium Pseudoalteromonas fuliginea PS47.,Acta Crystallographica Section F

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The structure of PfGH50B, an agarase from the marine bacterium Pseudoalteromonas fuliginea PS47.
Acta Crystallographica Section F ( IF 1.1 ) Pub Date : 2020-09-03 , DOI: 10.1107/s2053230x20010328
Benjamin Pluvinage ₁ , Craig S Robb ₁ , Roderick Jeffries ₁ , Alisdair B Boraston ₁

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The recently identified marine bacterium Pseudoalteromonas fuliginea sp. PS47 possesses a polysaccharide‐utilization locus dedicated to agarose degradation. In particular, it contains a gene (locus tag EU509_06755) encoding a β‐agarase that belongs to glycoside hydrolase family 50 (GH50), PfGH50B. The 2.0 Å resolution X‐ray crystal structure of PfGH50B reveals a rare complex multidomain fold that was found in two of the three previously determined GH50 structures. The structure comprises an N‐terminal domain with a carbohydrate‐binding module (CBM)‐like fold fused to a C‐terminal domain by a rigid linker. The CBM‐like domain appears to function by extending the catalytic groove of the enzyme. Furthermore, the PfGH50B structure highlights key structural features in the mobile loops that may function to restrict the degree of polymerization of the neoagaro‐oligosaccharide products and the enzyme processivity.

中文翻译：

PfGH50B 的结构，一种来自海洋细菌 Pseudoalteromonas fuliginea PS47 的琼脂酶。

最近发现的海洋细菌Pseudoalteromonas fuliginea sp。PS47 拥有专门用于琼脂糖降解的多糖利用位点。特别是，它包含编码属于糖苷水解酶家族 50 (GH50) Pf GH50B 的 β-琼脂酶的基因（基因座标签 EU509_06755）。Pf GH50B的 2.0 Å 分辨率 X 射线晶体结构揭示了一种罕见的复杂多域折叠，这种折叠在先前确定的三个 GH50 结构中的两个中被发现。该结构包含一个带有碳水化合物结合模块 (CBM) 样折叠的 N 端结构域，通过刚性接头与 C 端结构域融合。CBM 样结构域似乎通过延长酶的催化槽来发挥作用。此外，Pf GH50B 结构突出了移动环中的关键结构特征，这些特征可能限制新琼脂寡糖产物的聚合度和酶的持续合成能力。

更新日期：2020-09-03

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