2gdt: Difference between revisions
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'''NMR Structure of the nonstructural protein 1 (nsp1) from the SARS coronavirus'''<br /> | '''NMR Structure of the nonstructural protein 1 (nsp1) from the SARS coronavirus'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2GDT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. Full crystallographic information is available from [http:// | 2GDT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GDT OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: virus]] | [[Category: virus]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:02:07 2008'' | ||
Revision as of 10:02, 23 January 2008
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NMR Structure of the nonstructural protein 1 (nsp1) from the SARS coronavirus
Overview
The nonstructural protein 1 (nsp1) of the SARS coronavirus (CoV) 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 NMR structure of, nsp1(13-128), which represents a novel alpha/beta-fold formed by a mixed, parallel/antiparallel 6-stranded beta-barrel, an alpha-helix covering one, opening of the barrel, and a 310-helix alongside the barrel. We further, characterized the full-length 179-residue protein and show that the, polypeptide segments of residues 1-12 and 129-179 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 NMR Structure of the Replicase Nonstructural Protein 1 from the SARS Coronavirus., Almeida MS, Johnson MA, Herrmann T, Geralt M, Wuthrich K, J Virol. 2007 Jan 3;. PMID:17202208
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
