2cjq

From Proteopedia

(Difference between revisions)

Revision as of 06:56, 1 December 2021

Bovine viral diarrhea virus CP7-R12 RNA-dependent RNA polymerase

Structural highlights

2cjq is a 1 chain structure with sequence from Bvdv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2ajj, 2ajm, 2ajn, 2ajo
Activity:	RNA-directed RNA polymerase, with EC number 2.7.7.48
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[POLG_BVDVC] Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (By similarity). P7 forms a leader sequence to properly orient NS2 in the membrane (By similarity). Uncleaved NS2-3 is required for production of infectious virus. NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus. NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS4A is a cofactor for the NS3 protease activity (By similarity). RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Viral RNA-dependent RNA polymerases (RdRp) differ from DNA-dependent RNA polymerases, DNA-dependent DNA polymerases, and reverse transcriptases in that RdRps contain "fingertips" consisting of several polypeptide strands in the fingers domain interacting with the thumb domain. The crystal structure of bovine viral diarrhea virus (BVDV) RdRp containing an Asn438 duplication shows that the "N-terminal domain," which occurs only in pestiviruses such as BVDV, interacts with the polymerase component of the same polypeptide chain. This contrasts with the domain swapping observed in the previously determined structure of the BVDV NADL strain RdRp. By comparison with the NADL structure and through the use of biochemical data, it is possible that the N-terminal domain, in conjunction with the fingertips, is required to bind and assist the translocation of the RNA template. The partial disorder of the loop containing the additional Asn438 residue may explain the low replication rate of the recombinant compared with the wild-type virus.

The structure of bovine viral diarrhea virus RNA-dependent RNA polymerase and its amino-terminal domain.,Choi KH, Gallei A, Becher P, Rossmann MG Structure. 2006 Jul;14(7):1107-13. PMID:16843892^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Choi KH, Gallei A, Becher P, Rossmann MG. The structure of bovine viral diarrhea virus RNA-dependent RNA polymerase and its amino-terminal domain. Structure. 2006 Jul;14(7):1107-13. PMID:16843892 doi:10.1016/j.str.2006.05.020

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cjq"

@@ Line 3: / Line 3: @@
 <StructureSection load='2cjq' size='340' side='right'caption='[[2cjq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2cjq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bvdv Bvdv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CJQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2cjq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bvdv Bvdv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CJQ FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ajj|2ajj]], [[2ajm|2ajm]], [[2ajn|2ajn]], [[2ajo|2ajo]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ajj|2ajj]], [[2ajm|2ajm]], [[2ajn|2ajn]], [[2ajo|2ajo]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjq OCA], [http://pdbe.org/2cjq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cjq RCSB], [http://www.ebi.ac.uk/pdbsum/2cjq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjq ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjq OCA], [https://pdbe.org/2cjq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cjq RCSB], [https://www.ebi.ac.uk/pdbsum/2cjq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/POLG_BVDVC POLG_BVDVC]] Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (By similarity).  P7 forms a leader sequence to properly orient NS2 in the membrane (By similarity).  Uncleaved NS2-3 is required for production of infectious virus.  NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus.  NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase.  NS4A is a cofactor for the NS3 protease activity (By similarity).  RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.
+[[https://www.uniprot.org/uniprot/POLG_BVDVC POLG_BVDVC]] Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (By similarity).  P7 forms a leader sequence to properly orient NS2 in the membrane (By similarity).  Uncleaved NS2-3 is required for production of infectious virus.  NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus.  NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase.  NS4A is a cofactor for the NS3 protease activity (By similarity).  RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2cjq

From Proteopedia

Revision as of 06:56, 1 December 2021

Bovine viral diarrhea virus CP7-R12 RNA-dependent RNA polymerase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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