1s0v

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spinqualitylabelsall models 1s0v, resolution 3.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structural basis for substrate selection by T7 RNA polymerase

Overview

The mechanism by which nucleotide polymerases select the correct substrate, is of fundamental importance to the fidelity of DNA replication and, transcription. During the nucleotide addition cycle, pol I DNA polymerases, undergo the transition from a catalytically inactive "open" to an active, "closed" conformation. All known determinants of substrate selection are, associated with the "closed" state. To elucidate if this mechanism is, conserved in homologous single subunit RNA polymerases (RNAPs), we have, determined the structure of T7 RNAP elongation complex with the incoming, substrate analog. Surprisingly, the substrate specifically binds to RNAP, in the "open" conformation, where it is base paired with the acceptor, template base, while Tyr639 provides discrimination of ribose versus, deoxyribose substrates. The structure therefore suggests a novel, mechanism, in which the substrate selection occurs prior to the, isomerization to the catalytically active conformation. Modeling of, multisubunit RNAPs suggests that this mechanism might be universal for all, RNAPs.

About this Structure

1S0V is a Single protein structure of sequence from Bacteriophage t7 with MG and APC as ligands. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.

Reference

Structural basis for substrate selection by t7 RNA polymerase., Temiakov D, Patlan V, Anikin M, McAllister WT, Yokoyama S, Vassylyev DG, Cell. 2004 Feb 6;116(3):381-91. PMID:15016373

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