5t2t

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='5t2t' size='340' side='right' caption='[[5t2t]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
<StructureSection load='5t2t' size='340' side='right' caption='[[5t2t]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5t2t]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T2T FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5t2t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lcmv Lcmv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T2T FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N8:(2Z)-4-[1-BENZYL-4-(4-CHLOROBENZYL)PIPERIDIN-4-YL]-2-HYDROXY-4-OXOBUT-2-ENOIC+ACID'>0N8</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N8:(2Z)-4-[1-BENZYL-4-(4-CHLOROBENZYL)PIPERIDIN-4-YL]-2-HYDROXY-4-OXOBUT-2-ENOIC+ACID'>0N8</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L, KUE_IGS310002 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11623 LCMV])</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'>[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='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=5t2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t2t OCA], [http://pdbe.org/5t2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t2t RCSB], [http://www.ebi.ac.uk/pdbsum/5t2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t2t ProSAT]</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=5t2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t2t OCA], [http://pdbe.org/5t2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t2t RCSB], [http://www.ebi.ac.uk/pdbsum/5t2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t2t ProSAT]</span></td></tr>
Line 10: Line 11:
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A0A059U382_9VIRU A0A059U382_9VIRU]] RNA-dependent RNA polymerase which is responsible for replication and transcription of the viral RNA genome. During transcription, synthesizes 4 subgenomic RNAs, and assures their capping by a cap-snatching mechanism, in which cellular capped pre-mRNA are used to generate primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner.[PIRNR:PIRNR000836]
[[http://www.uniprot.org/uniprot/A0A059U382_9VIRU A0A059U382_9VIRU]] RNA-dependent RNA polymerase which is responsible for replication and transcription of the viral RNA genome. During transcription, synthesizes 4 subgenomic RNAs, and assures their capping by a cap-snatching mechanism, in which cellular capped pre-mRNA are used to generate primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner.[PIRNR:PIRNR000836]
 +
 +
==See Also==
 +
*[[RNA polymerase|RNA polymerase]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Lcmv]]
[[Category: RNA-directed RNA polymerase]]
[[Category: RNA-directed RNA polymerase]]
[[Category: Alvarez, K]]
[[Category: Alvarez, K]]
Line 20: Line 25:
[[Category: Endonuclease]]
[[Category: Endonuclease]]
[[Category: Inhibitor]]
[[Category: Inhibitor]]
-
[[Category: Lcmv]]
 
[[Category: Mammarenavirus]]
[[Category: Mammarenavirus]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 06:30, 18 April 2018

Crystal structure of Lymphocytic choriomeningitis mammarenavirus endonuclease bound to compound L742001

5t2t, resolution 1.97Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools