1hi8: Difference between revisions
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|PDB= 1hi8 |SIZE=350|CAPTION= <scene name='initialview01'>1hi8</scene>, resolution 2.5Å | |PDB= 1hi8 |SIZE=350|CAPTION= <scene name='initialview01'>1hi8</scene>, resolution 2.5Å | ||
|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> | |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> | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|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> | |||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
1HI8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | 1HI8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_phi6 Pseudomonas phage phi6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HI8 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http://www.ncbi.nlm.nih.gov/pubmed/11242087 11242087] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11242087 11242087] | ||
[[Category: | [[Category: Pseudomonas phage phi6]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bamford, D H.]] | [[Category: Bamford, D H.]] | ||
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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 | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:05:25 2008'' | ||
Revision as of 21:05, 30 March 2008
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| , resolution 2.5Å | |||||||
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| Sites: | , , and | ||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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