1gx6: Difference between revisions

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[[Image:1gx6.gif|left|200px]]<br /><applet load="1gx6" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1gx6.gif|left|200px]]
caption="1gx6, resolution 1.85&Aring;" />
 
'''HEPATITIS C VIRUS RNA POLYMERASE IN COMPLEX WITH UTP AND MANGANESE'''<br />
{{Structure
|PDB= 1gx6 |SIZE=350|CAPTION= <scene name='initialview01'>1gx6</scene>, resolution 1.85&Aring;
|SITE= <scene name='pdbsite=UT1:Mn+Binding+Site+For+Chain+A'>UT1</scene>
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=UTP:URIDINE 5'-TRIPHOSPHATE'>UTP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48]
|GENE=
}}
 
'''HEPATITIS C VIRUS RNA POLYMERASE IN COMPLEX WITH UTP AND MANGANESE'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1GX6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus_genotype_1b_(isolate_bk) Hepatitis c virus genotype 1b (isolate bk)] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=UTP:'>UTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] Known structural/functional Site: <scene name='pdbsite=UT1:Mn+Binding+Site+For+Chain+A'>UT1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GX6 OCA].  
1GX6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus_genotype_1b_(isolate_bk) Hepatitis c virus genotype 1b (isolate bk)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GX6 OCA].  


==Reference==
==Reference==
Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides., Bressanelli S, Tomei L, Rey FA, De Francesco R, J Virol. 2002 Apr;76(7):3482-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11884572 11884572]
Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides., Bressanelli S, Tomei L, Rey FA, De Francesco R, J Virol. 2002 Apr;76(7):3482-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11884572 11884572]
[[Category: Hepatitis c virus genotype 1b (isolate bk)]]
[[Category: Hepatitis c virus genotype 1b (isolate bk)]]
[[Category: RNA-directed RNA polymerase]]
[[Category: RNA-directed RNA polymerase]]
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[[Category: virus replication]]
[[Category: virus replication]]


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Revision as of 12:29, 20 March 2008

File:1gx6.gif


PDB ID 1gx6

Drag the structure with the mouse to rotate
, resolution 1.85Å
Sites:
Ligands: and
Activity: RNA-directed RNA polymerase, with EC number 2.7.7.48
Coordinates: save as pdb, mmCIF, xml



HEPATITIS C VIRUS RNA POLYMERASE IN COMPLEX WITH UTP AND MANGANESE


OverviewOverview

We report here the results of a systematic high-resolution X-ray crystallographic analysis of complexes of the hepatitis C virus (HCV) RNA polymerase with ribonucleoside triphosphates (rNTPs) and divalent metal ions. An unexpected observation revealed by this study is the existence of a specific rGTP binding site in a shallow pocket at the molecular surface of the enzyme, 30 A away from the catalytic site. This previously unidentified rGTP pocket, which lies at the interface between fingers and thumb, may be an allosteric regulatory site and could play a role in allowing alternative interactions between the two domains during a possible conformational change of the enzyme required for efficient initiation. The electron density map at 1.7-A resolution clearly shows the mode of binding of the guanosine moiety to the enzyme. In the catalytic site, density corresponding to the triphosphates of nucleotides bound to the catalytic metals was apparent in each complex with nucleotides. Moreover, a network of triphosphate densities was detected; these densities superpose to the corresponding moieties of the nucleotides observed in the initiation complex reported for the polymerase of bacteriophage phi6, strengthening the proposal that the two enzymes initiate replication de novo by similar mechanisms. No equivalent of the protein stacking platform observed for the priming nucleotide in the phi6 enzyme is present in HCV polymerase, however, again suggesting that a change in conformation of the thumb domain takes place upon template binding to allow for efficient de novo initiation of RNA synthesis.

About this StructureAbout this Structure

1GX6 is a Single protein structure of sequence from Hepatitis c virus genotype 1b (isolate bk). Full crystallographic information is available from OCA.

ReferenceReference

Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides., Bressanelli S, Tomei L, Rey FA, De Francesco R, J Virol. 2002 Apr;76(7):3482-92. PMID:11884572

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