2p1d
From Proteopedia
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|PDB= 2p1d |SIZE=350|CAPTION= <scene name='initialview01'>2p1d</scene>, resolution 2.90Å | |PDB= 2p1d |SIZE=350|CAPTION= <scene name='initialview01'>2p1d</scene>, resolution 2.90Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=5GP:GUANOSINE-5'-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
- | |GENE= NSP5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | |GENE= NSP5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11060 Dengue virus 2]) |
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1l9k|1L9K]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p1d OCA], [http://www.ebi.ac.uk/pdbsum/2p1d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2p1d RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
- | 2P1D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 2P1D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P1D OCA]. |
==Reference== | ==Reference== | ||
An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization., Egloff MP, Benarroch D, Selisko B, Romette JL, Canard B, EMBO J. 2002 Jun 3;21(11):2757-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12032088 12032088] | An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization., Egloff MP, Benarroch D, Selisko B, Romette JL, Canard B, EMBO J. 2002 Jun 3;21(11):2757-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12032088 12032088] | ||
- | [[Category: Dengue virus | + | [[Category: Dengue virus 2]] |
[[Category: RNA-directed RNA polymerase]] | [[Category: RNA-directed RNA polymerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Line 26: | Line 29: | ||
[[Category: Egloff, M P.]] | [[Category: Egloff, M P.]] | ||
[[Category: MSGP, Marseilles Structural Genomics Program.@.AFMB.]] | [[Category: MSGP, Marseilles Structural Genomics Program.@.AFMB.]] | ||
- | [[Category: | + | [[Category: dengue virus methyltransferase]] |
- | [[Category: | + | [[Category: marseilles structural genomics program @ afmb]] |
- | [[Category: | + | [[Category: msgp]] |
+ | [[Category: structural genomic]] | ||
+ | [[Category: viral enzymes involved in replication]] | ||
+ | [[Category: vizier]] | ||
[[Category: vizier. viral enzymes involved in replication]] | [[Category: vizier. viral enzymes involved in replication]] | ||
- | [[Category: vizier; viral enzymes involved in replication; dengue virus methyltransferase; structural genomics; marseilles structural genomics program @ afmb; msgp]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:26:49 2008'' |
Revision as of 01:26, 31 March 2008
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, resolution 2.90Å | |||||||
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Ligands: | , , | ||||||
Gene: | NSP5 (Dengue virus 2) | ||||||
Activity: | RNA-directed RNA polymerase, with EC number 2.7.7.48 | ||||||
Related: | 1L9K
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of dengue methyltransferase in complex with GTP and S-Adenosyl-L-homocysteine
Overview
Viruses represent an attractive system with which to study the molecular basis of mRNA capping and its relation to the RNA transcription machinery. The RNA-dependent RNA polymerase NS5 of flaviviruses presents a characteristic motif of S-adenosyl-L-methionine-dependent methyltransferases at its N-terminus, and polymerase motifs at its C-terminus. The crystal structure of an N-terminal fragment of Dengue virus type 2 NS5 is reported at 2.4 A resolution. We show that this NS5 domain includes a typical methyltransferase core and exhibits a (nucleoside-2'-O-)-methyltransferase activity on capped RNA. The structure of a ternary complex comprising S-adenosyl-L-homocysteine and a guanosine triphosphate (GTP) analogue shows that 54 amino acids N-terminal to the core provide a novel GTP-binding site that selects guanine using a previously unreported mechanism. Binding studies using GTP- and RNA cap-analogues, as well as the spatial arrangement of the methyltransferase active site relative to the GTP-binding site, suggest that the latter is a specific cap-binding site. As RNA capping is an essential viral function, these results provide a structural basis for the rational design of drugs against the emerging flaviviruses.
About this Structure
2P1D is a Single protein structure of sequence from Dengue virus 2. Full crystallographic information is available from OCA.
Reference
An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization., Egloff MP, Benarroch D, Selisko B, Romette JL, Canard B, EMBO J. 2002 Jun 3;21(11):2757-68. PMID:12032088
Page seeded by OCA on Mon Mar 31 04:26:49 2008
Categories: Dengue virus 2 | RNA-directed RNA polymerase | Single protein | Benarooch, D. | Egloff, M P. | MSGP, Marseilles Structural Genomics Program.@.AFMB. | Dengue virus methyltransferase | Marseilles structural genomics program @ afmb | Msgp | Structural genomic | Viral enzymes involved in replication | Vizier | Vizier. viral enzymes involved in replication