4ym7
From Proteopedia
RNA polymerase I structure with an alternative dimer hinge
Structural highlights
FunctionRPA1_YEAST DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity). Publication Abstract from PubMedRNA polymerase I (Pol I) is the central, 14-subunit enzyme that synthesizes the ribosomal RNA (rRNA) precursor in eukaryotic cells. The recent crystal structure of Pol I at 2.8 A resolution revealed two novel elements: the `expander' in the active-centre cleft and the `connector' that mediates Pol I dimerization [Engel et al. (2013), Nature (London), 502, 650-655]. Here, a Pol I structure in an alternative crystal form that was solved by molecular replacement using the original atomic Pol I structure is reported. The resulting alternative structure lacks the expander but still shows an expanded active-centre cleft. The neighbouring Pol I monomers form a homodimer with a relative orientation distinct from that observed previously, establishing the connector as a hinge between Pol I monomers. An alternative RNA polymerase I structure reveals a dimer hinge.,Kostrewa D, Kuhn CD, Engel C, Cramer P Acta Crystallogr D Biol Crystallogr. 2015 Sep 1;71(Pt 9):1850-5. doi:, 10.1107/S1399004715012651. Epub 2015 Aug 25. PMID:26327374[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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