2fyg
From Proteopedia
(New page: 200px<br /><applet load="2fyg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fyg, resolution 1.80Å" /> '''Crystal structure of...) |
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| - | [[Image:2fyg.gif|left|200px]]<br /><applet load="2fyg" size=" | + | [[Image:2fyg.gif|left|200px]]<br /><applet load="2fyg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fyg, resolution 1.80Å" /> | caption="2fyg, resolution 1.80Å" /> | ||
'''Crystal structure of NSP10 from Sars coronavirus'''<br /> | '''Crystal structure of NSP10 from Sars coronavirus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The severe acute respiratory syndrome coronavirus (SARS-CoV) possesses a | + | The severe acute respiratory syndrome coronavirus (SARS-CoV) possesses a large 29.7-kb positive-stranded RNA genome. The first open reading frame encodes replicase polyproteins 1a and 1ab, which are cleaved to generate 16 "nonstructural" proteins, nsp1 to nsp16, involved in viral replication and/or RNA processing. Among these, nsp10 plays a critical role in minus-strand RNA synthesis in a related coronavirus, murine hepatitis virus. Here, we report the crystal structure of SARS-CoV nsp10 at a resolution of 1.8 A as determined by single-wavelength anomalous dispersion using phases derived from hexatantalum dodecabromide. nsp10 is a single domain protein consisting of a pair of antiparallel N-terminal helices stacked against an irregular beta-sheet, a coil-rich C terminus, and two Zn fingers. nsp10 represents a novel fold and is the first structural representative of this family of Zn finger proteins found so far exclusively in coronaviruses. The first Zn finger coordinates a Zn2+ ion in a unique conformation. The second Zn finger, with four cysteines, is a distant member of the "gag-knuckle fold group" of Zn2+-binding domains and appears to maintain the structural integrity of the C-terminal tail. A distinct clustering of basic residues on the protein surface suggests a nucleic acid-binding function. Gel shift assays indicate that in isolation, nsp10 binds single- and double-stranded RNA and DNA with high-micromolar affinity and without obvious sequence specificity. It is possible that nsp10 functions within a larger RNA-binding protein complex. However, its exact role within the replicase complex is still not clear. |
==About this Structure== | ==About this Structure== | ||
| - | 2FYG 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] with ZN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2FYG 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] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Brooun, A.]] | [[Category: Brooun, A.]] | ||
| - | [[Category: Buchmeier, M | + | [[Category: Buchmeier, M J.]] |
[[Category: Griffith, M.]] | [[Category: Griffith, M.]] | ||
| - | [[Category: Joseph, J | + | [[Category: Joseph, J S.]] |
[[Category: Kuhn, P.]] | [[Category: Kuhn, P.]] | ||
[[Category: Moy, K.]] | [[Category: Moy, K.]] | ||
| - | [[Category: Neuman, B | + | [[Category: Neuman, B W.]] |
| - | [[Category: Saikatendu, K | + | [[Category: Saikatendu, K S.]] |
| - | [[Category: Stevens, R | + | [[Category: Stevens, R C.]] |
[[Category: Subramanian, V.]] | [[Category: Subramanian, V.]] | ||
[[Category: Velasquez, J.]] | [[Category: Velasquez, J.]] | ||
| - | [[Category: Yadav, M | + | [[Category: Yadav, M K.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:26:21 2008'' |
Revision as of 15:26, 21 February 2008
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Crystal structure of NSP10 from Sars coronavirus
Overview
The severe acute respiratory syndrome coronavirus (SARS-CoV) possesses a large 29.7-kb positive-stranded RNA genome. The first open reading frame encodes replicase polyproteins 1a and 1ab, which are cleaved to generate 16 "nonstructural" proteins, nsp1 to nsp16, involved in viral replication and/or RNA processing. Among these, nsp10 plays a critical role in minus-strand RNA synthesis in a related coronavirus, murine hepatitis virus. Here, we report the crystal structure of SARS-CoV nsp10 at a resolution of 1.8 A as determined by single-wavelength anomalous dispersion using phases derived from hexatantalum dodecabromide. nsp10 is a single domain protein consisting of a pair of antiparallel N-terminal helices stacked against an irregular beta-sheet, a coil-rich C terminus, and two Zn fingers. nsp10 represents a novel fold and is the first structural representative of this family of Zn finger proteins found so far exclusively in coronaviruses. The first Zn finger coordinates a Zn2+ ion in a unique conformation. The second Zn finger, with four cysteines, is a distant member of the "gag-knuckle fold group" of Zn2+-binding domains and appears to maintain the structural integrity of the C-terminal tail. A distinct clustering of basic residues on the protein surface suggests a nucleic acid-binding function. Gel shift assays indicate that in isolation, nsp10 binds single- and double-stranded RNA and DNA with high-micromolar affinity and without obvious sequence specificity. It is possible that nsp10 functions within a larger RNA-binding protein complex. However, its exact role within the replicase complex is still not clear.
About this Structure
2FYG is a Single protein structure of sequence from Human sars coronavirus with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs., Joseph JS, Saikatendu KS, Subramanian V, Neuman BW, Brooun A, Griffith M, Moy K, Yadav MK, Velasquez J, Buchmeier MJ, Stevens RC, Kuhn P, J Virol. 2006 Aug;80(16):7894-901. PMID:16873246
Page seeded by OCA on Thu Feb 21 17:26:21 2008
Categories: Human sars coronavirus | Single protein | Brooun, A. | Buchmeier, M J. | Griffith, M. | Joseph, J S. | Kuhn, P. | Moy, K. | Neuman, B W. | Saikatendu, K S. | Stevens, R C. | Subramanian, V. | Velasquez, J. | Yadav, M K. | GOL | ZN | Sars virus polyprotein non-structural protein nsp10 | Zinc finger
