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首页> 外文期刊>Journal of Molecular Biology >Crystal structure of the alginate (poly alpha-l-guluronate) lyase from Corynebacterium sp. at 1.2 A resolution.
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Crystal structure of the alginate (poly alpha-l-guluronate) lyase from Corynebacterium sp. at 1.2 A resolution.

机译：来自棒杆菌属的藻酸盐（聚α-1-古洛糖酸）裂解酶的晶体结构。在1.2 A分辨率下。

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摘要

The crystal structure of alginate (poly alpha-l-guluronate) lyase from Corynebacterium sp. (ALY-1) was determined at 1.2A resolution using the MAD method and bromide ions. The structure of ALY-1 is abundant in beta-strands and has a deep cleft, similar to the jellyroll beta-sandwich found in 1,3-1,4-beta-glucanase. The structure suggests that alginate molecules may penetrate into the cleft to interact with the catalytic site of ALY-1. The reported crystal structure of another type of alginate lyase, A1-III, differs from that of ALY-1 in that it consists almost entirely of alpha-helical structure. Nevertheless, the putative catalytic residues in both enzymes are positioned in space in nearly identical arrangements. This finding suggests that both alginate lyases may have evolved through convergent evolution.
机译：来自棒杆菌属的藻酸盐（聚α-1-古洛糖酸）裂解酶的晶体结构。使用MAD方法和溴离子以1.2A的分辨率测定（ALY-1）。 ALY-1的结构在β链中丰富并且具有深裂痕，类似于在1,3-1,4-β-葡聚糖酶中发现的果冻β-三明治。该结构表明藻酸盐分子可能会渗透到裂缝中，与ALY-1的催化位点相互作用。报道的另一种藻酸盐裂解酶A1-III的晶体结构与ALY-1的晶体结构的不同之处在于，它几乎完全由α-螺旋结构组成。然而，两种酶中推定的催化残基以几乎相同的排列定位在空间中。该发现表明两种藻酸盐裂解酶都可能通过融合进化而进化。

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