2hvg: Difference between revisions
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[[Image:2hvg.gif|left|200px]] | [[Image:2hvg.gif|left|200px]] | ||
'''Crystal Structure of Adenylosuccinate Lyase from Plasmodium Vivax''' | {{Structure | ||
|PDB= 2hvg |SIZE=350|CAPTION= <scene name='initialview01'>2hvg</scene>, resolution 2.30Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Adenylosuccinate_lyase Adenylosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.2 4.3.2.2] | |||
|GENE= | |||
}} | |||
'''Crystal Structure of Adenylosuccinate Lyase from Plasmodium Vivax''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2HVG is a [ | 2HVG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_vivax Plasmodium vivax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HVG OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17125854 17125854] | ||
[[Category: Adenylosuccinate lyase]] | [[Category: Adenylosuccinate lyase]] | ||
[[Category: Plasmodium vivax]] | [[Category: Plasmodium vivax]] | ||
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[[Category: alpha helical]] | [[Category: alpha helical]] | ||
[[Category: sgc]] | [[Category: sgc]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
[[Category: structural genomics consortium]] | [[Category: structural genomics consortium]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:22:02 2008'' | ||
Revision as of 18:22, 20 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Adenylosuccinate lyase, with EC number 4.3.2.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Adenylosuccinate Lyase from Plasmodium Vivax
OverviewOverview
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.
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
Page seeded by OCA on Thu Mar 20 17:22:02 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Adenylosuccinate lyase
- Plasmodium vivax
- Single protein
- Alam, Z.
- Arrowsmith, C H.
- Bochkarev, A.
- Dong, A.
- Edwards, A M.
- Hills, T.
- Hui, R.
- Kozieradzki, I.
- Lew, J.
- Qiu, W.
- Ren, H.
- SGC, Structural Genomics Consortium.
- Sundstrom, M.
- Vedadi, M.
- Wasney, G A.
- Weigelt, J.
- Wernimont, A K.
- SO4
- Alpha helical
- Sgc
- Structural genomic
- Structural genomics consortium