2po4

</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=2po4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2po4 OCA], [https://pdbe.org/2po4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2po4 RCSB], [https://www.ebi.ac.uk/pdbsum/2po4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2po4 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Coliphage N4 virion RNA polymerase (vRNAP), which is injected into the host upon infection, transcribes the phage early genes from promoters that have a 5-bp stem-3 nt loop hairpin structure. Here, we describe the 2.0-A resolution x-ray crystal structure of N4 mini-vRNAP, a member of the T7-like, single-unit RNAP family and the minimal component having all RNAP functions of the full-length vRNAP. The structure resembles a "fisted right hand" with Fingers, Palm and Thumb subdomains connected to an N-terminal domain. We established that the specificity loop extending from the Fingers along with W129 of the N-terminal domain play critical roles in hairpin-promoter recognition. A comparison with the structure of the T7 RNAP initiation complex reveals that the pathway of the DNA to the active site is blocked in the apo-form vRNAP, indicating that vRNAP must undergo a large-scale conformational change upon promoter DNA binding and explaining the highly restricted promoter specificity of vRNAP that is essential for phage early transcription.

X-ray crystal structure of the polymerase domain of the bacteriophage N4 virion RNA polymerase.,Murakami KS, Davydova EK, Rothman-Denes LB Proc Natl Acad Sci U S A. 2008 Mar 24;. PMID:18362338<ref>PMID:18362338</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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