RNA polymerase subunit H features a β-ribbon motif within a novel fold that is present in archaea and eukaryotes

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 nuclea...

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Bibliographic Details
Published in:	Journal of molecular biology Vol. 287; no. 4; pp. 753 - 760
Main Authors:	Thiru, Abarna, Hodach, Meri, Eloranta, Jyrki J, Kostourou, Vassiliki, Weinzierl, Robert O.J, Matthews, Stephen
Format:	Journal Article
Language:	English
Published:	England Elsevier Ltd 09-04-1999
Subjects:	Amino Acid Sequence archaea Base Sequence Crystallography, X-Ray DNA Primers DNA-Directed RNA Polymerases - chemistry Enzyme Stability Eukaryotic Cells - enzymology Humans Magnetic Resonance Spectroscopy Methanococcus - enzymology Methanococcus jannaschii Models, Molecular Molecular Sequence Data Protein Conformation Protein Folding Recombinant Proteins - chemistry RPB5 Sequence Homology, Amino Acid thermostability triple resonance NMR thermostability RPB5 triple resonance NMR archaea
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Summary:	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 β sheet that is flanked on one side by three short helices. The dominant feature is β-ribbon motif, which presents a hydrophobic, basic surface, and defines a general RNA polymerase architectural scaffold.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0022-2836 1089-8638
DOI:	10.1006/jmbi.1999.2638