1oks
From Proteopedia
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| - | [[Image:1oks. | + | [[Image:1oks.jpg|left|200px]]<br /><applet load="1oks" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1oks" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1oks, resolution 1.80Å" /> | caption="1oks, resolution 1.80Å" /> | ||
'''CRYSTAL STRUCTURE OF THE MEASLES VIRUS PHOSPHOPROTEIN XD DOMAIN'''<br /> | '''CRYSTAL STRUCTURE OF THE MEASLES VIRUS PHOSPHOPROTEIN XD DOMAIN'''<br /> | ||
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==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] | + | 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] Known structural/functional Site: <scene name='pdbsite=NHE:Nhe Binding Site For Chain A'>NHE</scene>. 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]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:48:44 2007'' |
Revision as of 15:38, 18 December 2007
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CRYSTAL STRUCTURE OF THE MEASLES VIRUS PHOSPHOPROTEIN XD DOMAIN
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 (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
1OKS is a Single protein structure of sequence from Measles virus with NHE as ligand. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein., Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, Longhi S, J Biol Chem. 2003 Nov 7;278(45):44567-73. Epub 2003 Aug 27. PMID:12944395
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