3c46: Difference between revisions
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<StructureSection load='3c46' size='340' side='right'caption='[[3c46]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3c46' size='340' side='right'caption='[[3c46]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3c46]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3c46]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_N4 Escherichia phage N4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C46 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2HP:DIHYDROGENPHOSPHATE+ION'>2HP</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c46 OCA], [https://pdbe.org/3c46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c46 RCSB], [https://www.ebi.ac.uk/pdbsum/3c46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c46 ProSAT]</span></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=3c46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c46 OCA], [https://pdbe.org/3c46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c46 RCSB], [https://www.ebi.ac.uk/pdbsum/3c46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c46 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/RPOLV_BPN4 RPOLV_BPN4] DNA-dependent RNA polymerase, which is injected into the host upon infection and transcribes the phage early genes from promoters that have a 5-bp stem-3 nt loop hairpin structure.<ref>PMID:18362338</ref> <ref>PMID:19061645</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia phage N4]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gleghorn | [[Category: Gleghorn ML]] | ||
[[Category: Murakami | [[Category: Murakami KS]] | ||
Revision as of 21:09, 1 November 2023
X-ray crystal structure of the N4 mini-vRNAP P2_7a promoter complex soaked with MgCl2X-ray crystal structure of the N4 mini-vRNAP P2_7a promoter complex soaked with MgCl2
Structural highlights
FunctionRPOLV_BPN4 DNA-dependent RNA polymerase, which is injected into the host upon infection and transcribes the phage early genes from promoters that have a 5-bp stem-3 nt loop hairpin structure.[1] [2] Publication Abstract from PubMedColiphage N4 virion-encapsidated RNA polymerase (vRNAP) is a member of the phage T7-like single-subunit RNA polymerase (RNAP) family. Its central domain (mini-vRNAP) contains all RNAP functions of the full-length vRNAP, which recognizes a 5 to 7 base pair stem and 3 nucleotide loop hairpin DNA promoter. Here, we report the X-ray crystal structures of mini-vRNAP bound to promoters. Mini-vRNAP uses four structural motifs to recognize DNA sequences at the hairpin loop and stem and to unwind DNA. Despite their low sequence similarity, three out of four motifs are shared with T7 RNAP that recognizes a double-stranded DNA promoter. The binary complex structure and results of engineered disulfide linkage experiments reveal that the plug and motif B loop, which block the access of template DNA to the active site in the apo-form mini-vRNAP, undergo a large-scale conformational change upon promoter binding, explaining the restricted promoter specificity that is critical for N4 phage early transcription. Structural basis for DNA-hairpin promoter recognition by the bacteriophage N4 virion RNA polymerase.,Gleghorn ML, Davydova EK, Rothman-Denes LB, Murakami KS Mol Cell. 2008 Dec 5;32(5):707-17. PMID:19061645[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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