2AIF

Crystal Structure of High Mobility Like Protein, NHP2, putative from Cryptosporidium parvum

2AIF の概要

• エントリーDOI: 10.2210/pdb2aif/pdb
• 分子名称: ribosomal protein L7A (2 entities in total)
• 機能のキーワード: ribosomal protein, high-mobility like protein, transcription factor, structural genomics, structural genomics consortium, sgc, dna binding protein, cytokine
• 由来する生物種: Cryptosporidium parvum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14472.49

構造登録者

Dong, A.,Zhao, Y.,Lew, J.,Alam, Z.,Melone, M.,Arrowsmith, C.H.,Edwards, A.M.,Weigelt, J.,Sundstrom, M.,Hui, R.,Bochkarev, A.,Artz, J.,Structural Genomics Consortium (SGC) (登録日: 2005-07-29, 公開日: 2005-08-09, 最終更新日: 2023-08-23)

主引用文献

Vedadi, M.,Lew, J.,Artz, J.,Amani, M.,Zhao, Y.,Dong, A.,Wasney, G.A.,Gao, M.,Hills, T.,Brokx, S.,Qiu, W.,Sharma, S.,Diassiti, A.,Alam, Z.,Melone, M.,Mulichak, A.,Wernimont, A.,Bray, J.,Loppnau, P.,Plotnikova, O.,Newberry, K.,Sundararajan, E.,Houston, S.,Walker, J.,Tempel, W.,Bochkarev, A.,Kozieradzki, I.,Edwards, A.,Arrowsmith, C.,Roos, D.,Kain, K.,Hui, R.
Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
Mol.Biochem.Parasitol., 151:100-110, 2007

PubMed Abstract: Parasites from the protozoan phylum Apicomplexa are responsible for diseases, such as malaria, toxoplasmosis and cryptosporidiosis, all of which have significantly higher rates of mortality and morbidity in economically underdeveloped regions of the world. Advances in vaccine development and drug discovery are urgently needed to control these diseases and can be facilitated by production of purified recombinant proteins from Apicomplexan genomes and determination of their 3D structures. To date, both heterologous expression and crystallization of Apicomplexan proteins have seen only limited success. In an effort to explore the effectiveness of producing and crystallizing proteins on a genome-scale using a standardized methodology, over 400 distinct Plasmodium falciparum target genes were chosen representing different cellular classes, along with select orthologues from four other Plasmodium species as well as Cryptosporidium parvum and Toxoplasma gondii. From a total of 1008 genes from the seven genomes, 304 (30.2%) produced purified soluble proteins and 97 (9.6%) crystallized, culminating in 36 crystal structures. These results demonstrate that, contrary to previous findings, a standardized platform using Escherichia coli can be effective for genome-scale production and crystallography of Apicomplexan proteins. Predictably, orthologous proteins from different Apicomplexan genomes behaved differently in expression, purification and crystallization, although the overall success rates of Plasmodium orthologues do not differ significantly. Their differences were effectively exploited to elevate the overall productivity to levels comparable to the most successful ongoing structural genomics projects: 229 of the 468 target genes produced purified soluble protein from one or more organisms, with 80 and 32 of the purified targets, respectively, leading to crystals and ultimately structures from one or more orthologues.

PubMed: 17125854
DOI: 10.1016/j.molbiopara.2006.10.011

実験手法

X-RAY DIFFRACTION (1.895 Å)