First Crystal Structure of Rubisco from a Green Alga,Chlamydomonas reinhardtii *
First Crystal Structure of Rubisco from a Green Alga,Chlamydomonas reinhardtii *
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来自绿藻莱茵衣藻的 Rubisco 的第一个晶体结构*
DOI：
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发表时间：
2001
影响因子：
4.8
通讯作者：
I. Andersson
中科院分区：
文献类型：
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作者：
T. C. Taylor;A. Backlund;Karin Bjorhall;R. J. Spreitzer;I. Andersson
从单细胞绿藻莱茵衣藻（Chlamydomonas reinhardtii）中提取的Rubisco（核酮糖1,5-二磷酸羧化酶/加氧酶）晶体结构以1.4 Å分辨率测定。总体而言，该结构与先前确定的L8S8 Rubisco酶的结构高度相似。最大的差异是在小亚基（βA-βB环）的β链A和β链B之间的环，该环比spinacia Rubisco的相应区域长6个氨基酸残基。βA-βB环中残基的突变已被证明会影响全酶的稳定性和催化性能。衣原体结构中包含的信息使我们能够对这些突变的影响进行更可靠的分析。小亚基的最后13个残基没有观察到电子密度，假设它们在晶体中是无序的。由于数据的高分辨率，一些翻译后的修饰在结构中是明确明显的。这些包括半胱氨酸和n端甲基化和脯氨酸4-羟基化。
The crystal structure of Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) from the unicellular green alga Chlamydomonas reinhardtii has been determined to 1.4 Å resolution. Overall, the structure shows high similarity to the previously determined structures of L8S8 Rubisco enzymes. The largest difference is found in the loop between β strands A and B of the small subunit (βA-βB loop), which is longer by six amino acid residues than the corresponding region in Rubisco fromSpinacia. Mutations of residues in the βA-βB loop have been shown to affect holoenzyme stability and catalytic properties. The information contained in the Chlamydomonasstructure enables a more reliable analysis of the effect of these mutations. No electron density was observed for the last 13 residues of the small subunit, which are assumed to be disordered in the crystal. Because of the high resolution of the data, some posttranslational modifications are unambiguously apparent in the structure. These include cysteine and N-terminal methylations and proline 4-hydroxylations.