2hvg: Difference between revisions

Revision as of 23:10, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2hvg.png

Template:STRUCTURE 2hvg

Crystal Structure of Adenylosuccinate Lyase from Plasmodium VivaxCrystal Structure of Adenylosuccinate Lyase from Plasmodium Vivax

Template:ABSTRACT PUBMED 17125854

About this StructureAbout this Structure

2HVG is a Single protein structure of sequence from Plasmodium vivax. Full crystallographic information is available from OCA.

ReferenceReference

Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms., Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, 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, Mol Biochem Parasitol. 2007 Jan;151(1):100-10. Epub 2006 Nov 13. PMID:17125854

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of Adenylosuccinate Lyase from Plasmodium Vivax'''
+===Crystal Structure of Adenylosuccinate Lyase from Plasmodium Vivax===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17125854}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17125854}}
 ==About this Structure==
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 [[Category: Structural genomic]]
 [[Category: Structural genomics consortium]]
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