Structural highlights
Function
RPO5_METJA DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The archaeal H and eukaryotic RPB5 RNA polymerase subunits are highly homologous and are likely to play a fundamental role in transcription that extends from archaea to humans. We report the structure of subunit H, in solution, from the archaeon Methanococcus jannaschii using multidimensional nuclear magnetic resonance. The structure reveals a novel fold containing a four-stranded mixed beta sheet that is flanked on one side by three short helices. The dominant feature is beta-ribbon motif, which presents a hydrophobic, basic surface, and defines a general RNA polymerase architectural scaffold.
RNA polymerase subunit H features a beta-ribbon motif within a novel fold that is present in archaea and eukaryotes.,Thiru A, Hodach M, Eloranta JJ, Kostourou V, Weinzierl RO, Matthews S J Mol Biol. 1999 Apr 9;287(4):753-60. PMID:10191143[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Thiru A, Hodach M, Eloranta JJ, Kostourou V, Weinzierl RO, Matthews S. RNA polymerase subunit H features a beta-ribbon motif within a novel fold that is present in archaea and eukaryotes. J Mol Biol. 1999 Apr 9;287(4):753-60. PMID:10191143 doi:10.1006/jmbi.1999.2638
