1hi8: Difference between revisions

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[[Image:1hi8.gif|left|200px]]
[[Image:1hi8.gif|left|200px]]


{{Structure
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|PDB= 1hi8 |SIZE=350|CAPTION= <scene name='initialview01'>1hi8</scene>, resolution 2.5&Aring;
The line below this paragraph, containing "STRUCTURE_1hi8", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=CA1:The+Three+Conserved+Active+Site+Aspartate'>CA1</scene>, <scene name='pdbsite=CA2:The+Three+Conserved+Active+Site+Aspartate'>CA2</scene>, <scene name='pdbsite=MG1:Mg+Binding+Site+For+Chain+A'>MG1</scene> and <scene name='pdbsite=MG2:Mg+Binding+Site+For+Chain+B'>MG2</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|ACTIVITY=
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|GENE=
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|DOMAIN=
{{STRUCTURE_1hi8| PDB=1hi8  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hi8 OCA], [http://www.ebi.ac.uk/pdbsum/1hi8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hi8 RCSB]</span>
}}


'''RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6'''
'''RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6'''
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[[Category: Makeyev, E V.]]
[[Category: Makeyev, E V.]]
[[Category: Stuart, D I.]]
[[Category: Stuart, D I.]]
[[Category: rna polymerase]]
[[Category: Rna polymerase]]
[[Category: viral polymerase]]
[[Category: Viral polymerase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:52:23 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:05:25 2008''

Revision as of 18:52, 2 May 2008

File:1hi8.gif

Template:STRUCTURE 1hi8

RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6


OverviewOverview

In most RNA viruses, genome replication and transcription are catalysed by a viral RNA-dependent RNA polymerase. Double-stranded RNA viruses perform these operations in a capsid (the polymerase complex), using an enzyme that can read both single- and double-stranded RNA. Structures have been solved for such viral capsids, but they do not resolve the polymerase subunits in any detail. Here we show that the 2 A resolution X-ray structure of the active polymerase subunit from the double-stranded RNA bacteriophage straight phi6 is highly similar to that of the polymerase of hepatitis C virus, providing an evolutionary link between double-stranded RNA viruses and flaviviruses. By crystal soaking and co-crystallization, we determined a number of other structures, including complexes with oligonucleotide and/or nucleoside triphosphates (NTPs), that suggest a mechanism by which the incoming double-stranded RNA is opened up to feed the template through to the active site, while the substrates enter by another route. The template strand initially overshoots, locking into a specificity pocket, and then, in the presence of cognate NTPs, reverses to form the initiation complex; this process engages two NTPs, one of which acts with the carboxy-terminal domain of the protein to prime the reaction. Our results provide a working model for the initiation of replication and transcription.

About this StructureAbout this Structure

1HI8 is a Single protein structure of sequence from Pseudomonas phage phi6. Full crystallographic information is available from OCA.

ReferenceReference

A mechanism for initiating RNA-dependent RNA polymerization., Butcher SJ, Grimes JM, Makeyev EV, Bamford DH, Stuart DI, Nature. 2001 Mar 8;410(6825):235-40. PMID:11242087 Page seeded by OCA on Fri May 2 18:52:23 2008

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