1hi1
From Proteopedia
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|PDB= 1hi1 |SIZE=350|CAPTION= <scene name='initialview01'>1hi1</scene>, resolution 3.0Å | |PDB= 1hi1 |SIZE=350|CAPTION= <scene name='initialview01'>1hi1</scene>, resolution 3.0Å | ||
|SITE= <scene name='pdbsite=AT1:Atp+Binding+Site+For+Chain+A'>AT1</scene>, <scene name='pdbsite=AT2:Atp+Binding+Site+For+Chain+B'>AT2</scene>, <scene name='pdbsite=AT3:Atp+Binding+Site+For+Chain+C'>AT3</scene>, <scene name='pdbsite=CA1:The+Three+Conserved+Active+Site+Aspartate'>CA1</scene>, <scene name='pdbsite=CA2:The+Three+Conserved+Active+Site+Aspartate'>CA2</scene> and <scene name='pdbsite=CA3:The+Three+Conserved+Active+Site+Aspartate'>CA3</scene> | |SITE= <scene name='pdbsite=AT1:Atp+Binding+Site+For+Chain+A'>AT1</scene>, <scene name='pdbsite=AT2:Atp+Binding+Site+For+Chain+B'>AT2</scene>, <scene name='pdbsite=AT3:Atp+Binding+Site+For+Chain+C'>AT3</scene>, <scene name='pdbsite=CA1:The+Three+Conserved+Active+Site+Aspartate'>CA1</scene>, <scene name='pdbsite=CA2:The+Three+Conserved+Active+Site+Aspartate'>CA2</scene> and <scene name='pdbsite=CA3:The+Three+Conserved+Active+Site+Aspartate'>CA3</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5 | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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[[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 23 12:05:27 2008'' |
Revision as of 10:05, 23 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6 PLUS BOUND NTP
Overview
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 Structure
1HI1 is a Single protein structure of sequence from Bacteriophage phi-6. Full crystallographic information is available from OCA.
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:11242087
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