1oks: Difference between revisions

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==Overview==
==Overview==
Measles virus is a negative-sense, single-stranded RNA virus belonging to, the Mononegavirales order which comprises several human pathogens such as, Ebola, Nipah, and Hendra viruses. The phosphoprotein of measles virus is a, modular protein consisting of an intrinsically disordered N-terminal, domain (Karlin, D., Longhi, S., Receveur, V., and Canard, B. (2002), Virology 296, 251-262) and of a C-terminal moiety (PCT) composed of, alternating disordered and globular regions. We report the crystal, structure of the extreme C-terminal domain (XD) of measles virus, phosphoprotein (aa 459-507) at 1.8 A resolution. We have previously, reported that the C-terminal domain of measles virus nucleoprotein, NTAIL, is intrinsically unstructured and undergoes induced folding in the, presence of PCT ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12944395 (full description)]]
Measles virus is a negative-sense, single-stranded RNA virus belonging to, the Mononegavirales order which comprises several human pathogens such as, Ebola, Nipah, and Hendra viruses. The phosphoprotein of measles virus is a, modular protein consisting of an intrinsically disordered N-terminal, domain (Karlin, D., Longhi, S., Receveur, V., and Canard, B. (2002), Virology 296, 251-262) and of a C-terminal moiety (PCT) composed of, alternating disordered and globular regions. We report the crystal, structure of the extreme C-terminal domain (XD) of measles virus, phosphoprotein (aa 459-507) at 1.8 A resolution. We have previously, reported that the C-terminal domain of measles virus nucleoprotein, NTAIL, is intrinsically unstructured and undergoes induced folding in the, presence of PCT (Longhi, S., Receveur-Brechot, V., Karlin, D., Johansson, K., Darbon, H., Bhella, D., Yeo, R., Finet, S., and Canard, B. (2003) J., Biol. Chem. 278, 18638-18648). Using far-UV circular dichroism, we show, that within PCT, XD is the region responsible for the induced folding of, NTAIL. The crystal structure of XD consists of three helices, arranged in, an anti-parallel triple-helix bundle. The surface of XD formed between, helices alpha2 and alpha3 displays a long hydrophobic cleft that might, provide a complementary hydrophobic surface to embed and promote folding, of the predicted alpha-helix of NTAIL. We present a tentative model of the, interaction between XD and NTAIL. These results, beyond presenting the, first measles virus protein structure, shed light both on the function of, the phosphoprotein at the molecular level and on the process of induced, folding.


==About this Structure==
==About this Structure==
1OKS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Measles_virus Measles virus]] with NHE as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48]]. Structure known Active Site: NHE. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OKS OCA]].  
1OKS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Measles_virus Measles virus] with NHE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] Structure known Active Site: NHE. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OKS OCA].  


==Reference==
==Reference==
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[[Category: transferase]]
[[Category: transferase]]


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