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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structures of the -class carbonic anhydrase homologue YrdA suggest a possible allosteric switch
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Structures of the -class carbonic anhydrase homologue YrdA suggest a possible allosteric switch

机译：海尔集团的结构碳酸酐酶同系物YrdA建议一个可能的变构开关

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摘要

The YrdA protein shows high sequence similarity to -class carbonic anhydrase (-CA) proteins and is classified as part of the -CA protein family. However, its function has not been fully elucidated as it lacks several of the conserved residues that are considered to be necessary for -CA catalysis. Interestingly, a homologue of -CA from Methanosarcina thermophila and a Β-carboxysomal -CA from a Β-cyano-bacterium have shown that these catalytic residues are not always conserved in -CAs. The crystal structure of YrdA from Escherichia coli (ecYrdA) is reported here in two crystallographic forms. The overall structure of ecYrdA is also similar to those of the -CAs. One loop around the putative catalytic site shows a number of alternative conformations. A His residue (His70) on this loop coordinates with, or is reoriented from, the catalytic Zn 2+ ion; this is similar to the conformations mediated by an Asp residue on the catalytic loops of Β-CA proteins. One Trp residue (Trp171) also adopts two alternative conformations that may be related to the spatial positions of the catalytic loop. Even though significant CA activity could not be detected using purified ecYrdA, these structural features have potential functional implications for -CA-related proteins.
机译：YrdA蛋白质显示高序列相似性海尔集团碳酸酐酶(ca)蛋白质和归类为ca蛋白家族的一部分。然而,它的功能尚未完全阐明它缺少几个守恒的残留,被认为是必要的ca催化。从甲烷八叠球菌属thermophila和Β-carboxysomal ca从Β蓝藻细菌表明,这些催化残基不是总是在中科院守恒。YrdA从大肠杆菌(ecYrdA)在两种晶体形式报告。总体结构的ecYrdA也类似中科院。催化部位显示了一个数量的选择构象。坐标,或者是调整催化锌2 +离子;构象由一个Asp的残渣催化循环的Βca蛋白。(Trp171)也采用两种可能与空间构象位置的催化循环。重要的CA活动不能被检测到使用纯化ecYrdA,这些结构特点有潜在功能的影响吗-CA-related蛋白质。

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