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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2fyg.gif|left|200px]]<br /><applet load="2fyg" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2fyg, resolution 1.80&Aring;" />
caption="2fyg, resolution 1.80&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FYG OCA].  
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.J.]]
[[Category: Buchmeier, M J.]]
[[Category: Griffith, M.]]
[[Category: Griffith, M.]]
[[Category: Joseph, J.S.]]
[[Category: Joseph, J S.]]
[[Category: Kuhn, P.]]
[[Category: Kuhn, P.]]
[[Category: Moy, K.]]
[[Category: Moy, K.]]
[[Category: Neuman, B.W.]]
[[Category: Neuman, B W.]]
[[Category: Saikatendu, K.S.]]
[[Category: Saikatendu, K S.]]
[[Category: Stevens, R.C.]]
[[Category: Stevens, R C.]]
[[Category: Subramanian, V.]]
[[Category: Subramanian, V.]]
[[Category: Velasquez, J.]]
[[Category: Velasquez, J.]]
[[Category: Yadav, M.K.]]
[[Category: Yadav, M K.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: zinc finger]]
[[Category: zinc finger]]


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