1uvl
From Proteopedia
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|PDB= 1uvl |SIZE=350|CAPTION= <scene name='initialview01'>1uvl</scene>, resolution 2.00Å | |PDB= 1uvl |SIZE=350|CAPTION= <scene name='initialview01'>1uvl</scene>, resolution 2.00Å | ||
|SITE= <scene name='pdbsite=AC1:Mn+Binding+Site+For+Chain+E'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mn+Binding+Site+For+Chain+E'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | + | |LIGAND= <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uvl OCA], [http://www.ebi.ac.uk/pdbsum/1uvl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uvl RCSB]</span> | ||
}} | }} | ||
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[[Category: Salgado, P S.]] | [[Category: Salgado, P S.]] | ||
[[Category: Stuart, D I.]] | [[Category: Stuart, D I.]] | ||
| - | + | [[Category: oligonucleotide polymerase,transcription]] | |
| - | [[Category: oligonucleotide polymerase]] | + | |
[[Category: rna-dependent rna polymerase]] | [[Category: rna-dependent rna polymerase]] | ||
[[Category: structural protein]] | [[Category: structural protein]] | ||
| - | [[Category: transcription]] | ||
| - | ''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 00:15:52 2008'' |
Revision as of 21:15, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURAL BASIS FOR RNA SPECIFICITY AND CA2 INHIBITION OF AN RNA-DEPENDENT RNA POLYMERASE PHI6P2 WITH 5NT RNA CONFORMATION B
Overview
The RNA-dependent RNA polymerase of bacteriophage phi6 transcribes mRNA from the three segments of the dsRNA viral genome. We have cocrystallized RNA oligonucleotides with the polymerase, revealing the mode of binding of RNA templates. This binding is somewhat different from that previously seen for DNA oligomers, leading to additional RNA-protein hydrogen bonds, consistent with a preference for RNA. Activation of the RNA/polymerase complex by the addition of substrate and Mg2+ initiates a single round of reaction within the crystal to form a dead-end complex that partially collapses within the enzyme active site. By replacing Mg2+ with Ca2+, we have been able to capture the inhibited complex which shows distortion that explains the structural basis for the inhibition of such polymerases by Ca2+.
About this Structure
1UVL is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
The structural basis for RNA specificity and Ca2+ inhibition of an RNA-dependent RNA polymerase., Salgado PS, Makeyev EV, Butcher SJ, Bamford DH, Stuart DI, Grimes JM, Structure. 2004 Feb;12(2):307-16. PMID:14962391
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