2gdt
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The nonstructural protein 1 (nsp1) of the | + | The nonstructural protein 1 (nsp1) of the severe acute respiratory syndrome coronavirus has 179 residues and is the N-terminal cleavage product of the viral replicase polyprotein that mediates RNA replication and processing. The specific function of nsp1 is not known. Here we report the nuclear magnetic resonance structure of the nsp1 segment from residue 13 to 128, which represents a novel alpha/beta-fold formed by a mixed parallel/antiparallel six-stranded beta-barrel, an alpha-helix covering one opening of the barrel, and a 3(10)-helix alongside the barrel. We further characterized the full-length 179-residue protein and show that the polypeptide segments of residues 1 to 12 and 129 to 179 are flexibly disordered. The structure is analyzed in a search for possible correlations with the recently reported activity of nsp1 in the degradation of mRNA. |
==About this Structure== | ==About this Structure== | ||
| Line 10: | Line 10: | ||
==Reference== | ==Reference== | ||
| - | Novel | + | Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus., Almeida MS, Johnson MA, Herrmann T, Geralt M, Wuthrich K, J Virol. 2007 Apr;81(7):3151-61. Epub 2007 Jan 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17202208 17202208] |
[[Category: Sars coronavirus]] | [[Category: Sars coronavirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Almeida, M | + | [[Category: Almeida, M S.]] |
| - | [[Category: Buchmeier, M | + | [[Category: Buchmeier, M J.]] |
[[Category: Geralt, M.]] | [[Category: Geralt, M.]] | ||
[[Category: Herrmann, T.]] | [[Category: Herrmann, T.]] | ||
| - | [[Category: JCSG, Joint | + | [[Category: JCSG, Joint Center for Structural Genomics.]] |
| - | [[Category: Johnson, M | + | [[Category: Johnson, M A.]] |
[[Category: Joseph, J.]] | [[Category: Joseph, J.]] | ||
[[Category: Kuhn, P.]] | [[Category: Kuhn, P.]] | ||
| - | [[Category: Neuman, B | + | [[Category: Neuman, B W.]] |
[[Category: Saikatendu, K.]] | [[Category: Saikatendu, K.]] | ||
| - | [[Category: Stevens, R | + | [[Category: Stevens, R C.]] |
| - | [[Category: Subramanian, R | + | [[Category: Subramanian, R C.]] |
| - | [[Category: Wilson, I | + | [[Category: Wilson, I A.]] |
[[Category: Wuthrich, K.]] | [[Category: Wuthrich, K.]] | ||
[[Category: alpha-beta]] | [[Category: alpha-beta]] | ||
| Line 41: | Line 41: | ||
[[Category: virus]] | [[Category: virus]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:30:51 2008'' |
Revision as of 15:30, 21 February 2008
|
NMR Structure of the nonstructural protein 1 (nsp1) from the SARS coronavirus
Overview
The nonstructural protein 1 (nsp1) of the severe acute respiratory syndrome coronavirus has 179 residues and is the N-terminal cleavage product of the viral replicase polyprotein that mediates RNA replication and processing. The specific function of nsp1 is not known. Here we report the nuclear magnetic resonance structure of the nsp1 segment from residue 13 to 128, which represents a novel alpha/beta-fold formed by a mixed parallel/antiparallel six-stranded beta-barrel, an alpha-helix covering one opening of the barrel, and a 3(10)-helix alongside the barrel. We further characterized the full-length 179-residue protein and show that the polypeptide segments of residues 1 to 12 and 129 to 179 are flexibly disordered. The structure is analyzed in a search for possible correlations with the recently reported activity of nsp1 in the degradation of mRNA.
About this Structure
2GDT is a Single protein structure of sequence from Sars coronavirus. Full crystallographic information is available from OCA.
Reference
Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus., Almeida MS, Johnson MA, Herrmann T, Geralt M, Wuthrich K, J Virol. 2007 Apr;81(7):3151-61. Epub 2007 Jan 3. PMID:17202208
Page seeded by OCA on Thu Feb 21 17:30:51 2008
Categories: Sars coronavirus | Single protein | Almeida, M S. | Buchmeier, M J. | Geralt, M. | Herrmann, T. | JCSG, Joint Center for Structural Genomics. | Johnson, M A. | Joseph, J. | Kuhn, P. | Neuman, B W. | Saikatendu, K. | Stevens, R C. | Subramanian, R C. | Wilson, I A. | Wuthrich, K. | Alpha-beta | Beta-barrel | Hydrolase | Jcsg | Joint center for structural genomics | Leader protein | Nmr | Protein structure initiative | Psi-2 | Replicase | Structural genomics | Viral protein | Virus
