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1ysy

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(New page: 200px<br /><applet load="1ysy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ysy" /> '''NMR Structure of the nonstructural Protein 7...)
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[[Image:1ysy.gif|left|200px]]<br /><applet load="1ysy" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ysy.gif|left|200px]]<br /><applet load="1ysy" size="350" color="white" frame="true" align="right" spinBox="true"
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'''NMR Structure of the nonstructural Protein 7 (nsP7) from the SARS CoronaVirus'''<br />
'''NMR Structure of the nonstructural Protein 7 (nsP7) from the SARS CoronaVirus'''<br />
==Overview==
==Overview==
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Here, we report the three-dimensional structure of severe acute, respiratory syndrome coronavirus (SARS-CoV) nsP7, a component of the, SARS-CoV replicase polyprotein. The coronavirus replicase carries out, regulatory tasks involved in the maintenance, transcription, and, replication of the coronavirus genome. nsP7 was found to assume a compact, architecture in solution, which is comprised primarily of helical, secondary structures. Three helices (alpha2 to alpha4) form a flat, up-down-up antiparallel alpha-helix sheet. The N-terminal segment of, residues 1 to 22, containing two turns of alpha-helix and one turn of, 3(10)-helix, is packed across the surface of alpha2 and alpha3 in the, helix sheet, with the alpha-helical region oriented at a 60 degrees angle, relative to alpha2 and alpha3. The surface charge distribution is, pronouncedly asymmetrical, with the flat surface of the helical sheet, showing a large negatively charged region adjacent to a large hydrophobic, patch and the opposite side containing a positively charged groove that, extends along the helix alpha1. Each of these three areas is thus, implicated as a potential site for protein-protein interactions.
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Here, we report the three-dimensional structure of severe acute respiratory syndrome coronavirus (SARS-CoV) nsP7, a component of the SARS-CoV replicase polyprotein. The coronavirus replicase carries out regulatory tasks involved in the maintenance, transcription, and replication of the coronavirus genome. nsP7 was found to assume a compact architecture in solution, which is comprised primarily of helical secondary structures. Three helices (alpha2 to alpha4) form a flat up-down-up antiparallel alpha-helix sheet. The N-terminal segment of residues 1 to 22, containing two turns of alpha-helix and one turn of 3(10)-helix, is packed across the surface of alpha2 and alpha3 in the helix sheet, with the alpha-helical region oriented at a 60 degrees angle relative to alpha2 and alpha3. The surface charge distribution is pronouncedly asymmetrical, with the flat surface of the helical sheet showing a large negatively charged region adjacent to a large hydrophobic patch and the opposite side containing a positively charged groove that extends along the helix alpha1. Each of these three areas is thus implicated as a potential site for protein-protein interactions.
==About this Structure==
==About this Structure==
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1YSY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YSY OCA].
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1YSY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YSY OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Herrmann, T.]]
[[Category: Herrmann, T.]]
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[[Category: JCSG, Joint.Center.for.Structural.Genomics.]]
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[[Category: JCSG, Joint Center for Structural Genomics.]]
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[[Category: Johnson, M.A.]]
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[[Category: Johnson, M A.]]
[[Category: Kuhn, P.]]
[[Category: Kuhn, P.]]
[[Category: Peti, W.]]
[[Category: Peti, W.]]
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[[Category: Stevens, R.C.]]
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[[Category: Stevens, R C.]]
[[Category: Wuthrich, K.]]
[[Category: Wuthrich, K.]]
[[Category: helix bundle]]
[[Category: helix bundle]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:01:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:46 2008''

Revision as of 14:08, 21 February 2008


1ysy

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NMR Structure of the nonstructural Protein 7 (nsP7) from the SARS CoronaVirus

Overview

Here, we report the three-dimensional structure of severe acute respiratory syndrome coronavirus (SARS-CoV) nsP7, a component of the SARS-CoV replicase polyprotein. The coronavirus replicase carries out regulatory tasks involved in the maintenance, transcription, and replication of the coronavirus genome. nsP7 was found to assume a compact architecture in solution, which is comprised primarily of helical secondary structures. Three helices (alpha2 to alpha4) form a flat up-down-up antiparallel alpha-helix sheet. The N-terminal segment of residues 1 to 22, containing two turns of alpha-helix and one turn of 3(10)-helix, is packed across the surface of alpha2 and alpha3 in the helix sheet, with the alpha-helical region oriented at a 60 degrees angle relative to alpha2 and alpha3. The surface charge distribution is pronouncedly asymmetrical, with the flat surface of the helical sheet showing a large negatively charged region adjacent to a large hydrophobic patch and the opposite side containing a positively charged groove that extends along the helix alpha1. Each of these three areas is thus implicated as a potential site for protein-protein interactions.

About this Structure

1YSY is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.

Reference

Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7., Peti W, Johnson MA, Herrmann T, Neuman BW, Buchmeier MJ, Nelson M, Joseph J, Page R, Stevens RC, Kuhn P, Wuthrich K, J Virol. 2005 Oct;79(20):12905-13. PMID:16188992

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