1UVM

The structural basis for RNA specificity and Ca2 inhibition of an RNA-dependent RNA polymerase phi6p2 with 5NT RNA conformation A

Summary for 1UVM

• Entry DOI: 10.2210/pdb1uvm/pdb
• Related: 1HHS 1HHT 1HI0 1HI1 1HI8 1UVI 1UVJ 1UVK 1UVL 1UVN
• Descriptor: RNA-directed RNA polymerase, 5'-R(*UP*UP*UP*CP*CP)-3', MANGANESE (II) ION, ... (4 entities in total)
• Functional Keywords: polymerase, transferase, nucleotidyltransferase, transcription
• Biological source: Pseudomonas phage phi6 (Bacteriophage phi-6); More
• Cellular location: Virion: P11124
• Total number of polymer chains: 6
• Total formula weight: 229326.14

Authors

Salgado, P.S.,Makeyev, E.V.,Butcher, S.,Bamford, D.,Stuart, D.I.,Grimes, J.M. (deposition date: 2004-01-21, release date: 2004-02-19, Last modification date: 2023-12-13)

Primary citation

Salgado, P.S.,Makeyev, E.V.,Butcher, S.J.,Bamford, D.H.,Stuart, D.I.,Grimes, J.M.
The structural basis for RNA specificity and Ca2+ inhibition of an RNA-dependent RNA polymerase.
Structure, 12:307-316, 2004

PubMed Abstract: 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+.

PubMed: 14962391
DOI: 10.1016/j.str.2004.01.012

Experimental method

X-RAY DIFFRACTION (2 Å)