1hi0: Difference between revisions

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|PDB= 1hi0 |SIZE=350|CAPTION= <scene name='initialview01'>1hi0</scene>, resolution 3.0&Aring;
|PDB= 1hi0 |SIZE=350|CAPTION= <scene name='initialview01'>1hi0</scene>, resolution 3.0&Aring;
|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=CA3:The+Three+Conserved+Active+Site+Aspartate'>CA3</scene>, <scene name='pdbsite=GP1:Gtp+Binding+Site+For+Residue+P666'>GP1</scene>, <scene name='pdbsite=GP2:Gtp+Binding+Site+For+Residue+P667'>GP2</scene>, <scene name='pdbsite=GQ1:Gtp+Binding+Site+For+Residue+Q666'>GQ1</scene>, <scene name='pdbsite=GQ2:Gtp+Binding+Site+For+Residue+Q667'>GQ2</scene>, <scene name='pdbsite=GR1:Gtp+Binding+Site+For+Residue+R666'>GR1</scene> and <scene name='pdbsite=GR2:Gtp+Binding+Site+For+Residue+R667'>GR2</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=CA3:The+Three+Conserved+Active+Site+Aspartate'>CA3</scene>, <scene name='pdbsite=GP1:Gtp+Binding+Site+For+Residue+P666'>GP1</scene>, <scene name='pdbsite=GP2:Gtp+Binding+Site+For+Residue+P667'>GP2</scene>, <scene name='pdbsite=GQ1:Gtp+Binding+Site+For+Residue+Q666'>GQ1</scene>, <scene name='pdbsite=GQ2:Gtp+Binding+Site+For+Residue+Q667'>GQ2</scene>, <scene name='pdbsite=GR1:Gtp+Binding+Site+For+Residue+R666'>GR1</scene> and <scene name='pdbsite=GR2:Gtp+Binding+Site+For+Residue+R667'>GR2</scene>
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GTP:GUANOSINE-5&#39;-TRIPHOSPHATE'>GTP</scene>
|LIGAND= <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=GTP:GUANOSINE-5&#39;-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1hhs|1HHS]], [[1hht|1HHT]], [[1hi1|1HI1]], [[1hi8|1HI8]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hi0 OCA], [http://www.ebi.ac.uk/pdbsum/1hi0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hi0 RCSB]</span>
}}
}}


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==About this Structure==
==About this Structure==
1HI0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_phi-6 Bacteriophage phi-6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HI0 OCA].  
1HI0 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=1HI0 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: Bacteriophage phi-6]]
[[Category: Pseudomonas phage phi6]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bamford, D H.]]
[[Category: Bamford, D H.]]
Line 27: Line 30:
[[Category: Makeyev, E V.]]
[[Category: Makeyev, E V.]]
[[Category: Stuart, D I.]]
[[Category: Stuart, D I.]]
[[Category: GTP]]
[[Category: MG]]
[[Category: MN]]
[[Category: rna polymerase]]
[[Category: rna polymerase]]
[[Category: viral polymerase]]
[[Category: viral polymerase]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:05:21 2008''

Revision as of 21:05, 30 March 2008

File:1hi0.gif


PDB ID 1hi0

Drag the structure with the mouse to rotate
, resolution 3.0Å
Sites: , , , , , , , and
Ligands: , , , ,
Related: 1HHS, 1HHT, 1HI1, 1HI8


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6 PLUS INITIATION COMPLEX


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

1HI0 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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